Information on EC 1.8.99.2 - adenylyl-sulfate reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.8.99.2
-
RECOMMENDED NAME
GeneOntology No.
adenylyl-sulfate reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
-
-
-
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
catalysis involves a nucleophilic attack of the N5-atom of reduced FAD on the sulfur atom of the enzyme
O28603
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
show the reaction diagram
mechanism
Desulfovibrio vulgaris Hildenborough
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
-
-
redox reaction
-
-
-
-
redox reaction
-
-
redox reaction
-
-
reduction
-
-
-
-
reduction
-
-
reduction
-
dissimilatory sulfate reduction
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Microbial metabolism in diverse environments
-
sulfate reduction IV (dissimilatory)
-
sulfate reduction V (dissimilatory)
-
sulfite oxidation II
-
sulfite oxidation III
-
Sulfur metabolism
-
SYSTEMATIC NAME
IUBMB Comments
AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming)
An iron flavoprotein (FAD). Methyl viologen can act as acceptor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5'-adenylyl sulfate reductase
O81350
-
5'-adenylylsulfate reductase
-
-
5-adenylylsulfate reductase
-
-
AcAPR1
-
-
adenosine 5'-phosphosulfate reductase
-
-
-
-
adenosine 5'-phosphosulfate reductase
-
-
adenosine 5'-phosphosulfate reductase
-
-
adenosine 5'-phosphosulfate reductase
O28603
-
adenosine 5'-phosphosulfate reductase
-
-
adenosine 5'-phosphosulfate reductase
-
-
adenosine 5'-phosphosulfate reductase
-
-
adenosine 5'-phosphosulfate reductase
-
-
adenosine phosphosulfate reductase
-
-
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
O33996, O33997
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
Candidatus Ruthia magnifica CM
-
-
-
adenosine-5'-phosphosulfate reductase
A8JZB6, A8JZB7
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
Chlorobaculum tepidum TLS
-
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
-
-
-
adenosine-5'-phosphosulfate reductase
A8JZB0, A8JZB1
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
-
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
A8JZC4, A8JZC5
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
A8JZB8, A8JZB9
-
adenosine-5'-phosphosulfate reductase
Pelodictyon clathratiforme BU-1
-
-
-
adenosine-5'-phosphosulfate reductase
-
-
adenosine-5'-phosphosulfate reductase
A8JZC0, A8JZC1
-
adenosine-5'-phosphosulfate reductase
A8JZC8, A8JZC9
-
adenosine-5'-phosphosulfate reductase
A8JZC6, A8JZC7
-
adenosine-5'-phosphosulfate reductase
F6KEW4 and F6KEW3
-
adenylyl sulfate reductase
-
-
adenylylsulfate reductase
O28603 and O28604
-
adenylylsulfate reductase
Archaeoglobus fulgidus ATCC 49558
O28603 and O28604
-
-
adenylylsulfate reductase
-
-
adenylylsulfate reductase
B8PS61 and B8DS74
-
adenylylsulfate reductase
Desulfovibrio vulgaris Miyazaki F
B8PS61 and B8DS74
-
-
adenylylsulphate reductase
Q59339 and Q59338
-
AdoPSO4 reductase
-
-
-
-
AMP,sulfite:flavin oxidoreductase
-
-
-
-
APR1
-
isoform
APR2
-
isoform
APR3
-
isoform
AprB
F6KEW4 and F6KEW3
small subunit
AprBA
Candidatus Ruthia magnifica CM
-
-
-
AprBA
A8JZB6, A8JZB7
-
AprBA
Q8KE28
-
AprBA
Chlorobaculum tepidum TLS
-
-
-
AprBA
A8JZB0, A8JZB1
-
AprBA
Desulfobulbus sp. MLMS-1
-
-
-
AprBA
Desulfovibrio vulgaris Hildenborough
Q72DT3
-
-
AprBA
A8JZC4, A8JZC5
-
AprBA
B5QSJ0
-
AprBA
-, A8JZB8, A8JZB9
-
AprBA
Pelodictyon clathratiforme BU-1
-
-
-
AprBA
Q5VLA6, Q5VLA7
-
AprBA
A8JZC0, A8JZC1
-
AprBA
A8JZC8, A8JZC9
-
AprBA
A8JZC6, A8JZC7
-
APS reductase
-
-
-
-
APS reductase
-
-
APS reductase
O33996, O33997
-
APS reductase
-
-
APS reductase
O28603
-
APS reductase
O28603 and O28604
-
APS reductase
Q59339 and Q59338
-
APS reductase
Candidatus Ruthia magnifica CM
-
-
-
APS reductase
A8JZB6, A8JZB7
-
APS reductase
-
-
APS reductase
Chlorobaculum tepidum TLS
-
-
-
APS reductase
-
-
-
APS reductase
A8JZB0, A8JZB1
-
APS reductase
-
-
-
APS reductase
-
-
APS reductase
-
-
APS reductase
B8PS61 and B8DS74
-
APS reductase
Desulfovibrio vulgaris Miyazaki F
B8PS61 and B8DS74
-
-
APS reductase
-
-
APS reductase
A8JZC4, A8JZC5
-
APS reductase
A8JZB8, A8JZB9
-
APS reductase
Pelodictyon clathratiforme BU-1
-
-
-
APS reductase
-
-
APS reductase
A8JZC0, A8JZC1
-
APS reductase
A8JZC8, A8JZC9
-
APS reductase
A8JZC6, A8JZC7
-
APS reductase
F6KEW4 and F6KEW3
-
APS-reductase
-
-
-
-
APSR
O28603 and O28604
-
APSR
Archaeoglobus fulgidus ATCC 49558
O28603 and O28604
-
-
dissimilatory APS reductase
O33996
-
dissimilatory APS reductase
-
-
-
dissimilatory APS reductase
Q9L768
-
dissimilatory APS reductase
B5QSJ0
-
dissimilatory APS reductase
-
-
dissimilatory APS reductase
A0LH39
-
dissimilatory APS reductase
Q5VLA6, Q5VLA7
-
dissimilatory APS reductases
Q8KE28
-
dissimilatory APS reductases
-
-
dissimilatory APS reductases
Desulfobulbus sp. MLMS-1
-
-
-
dissimilatory APS reductases
-
-
dissimilatory APS reductases
Q72DT3
-
dissimilatory APS reductases
Desulfovibrio vulgaris Hildenborough
Q72DT3
-
-
EiAPR
O81350
-
FAD, FeS-enzyme adenosine-5'-phosphosulfate reductase
-
-
LMAPR
-
-
reductase, adenylylsulfate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-75-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
aprA; gene aprA
UniProt
Manually annotated by BRENDA team
aprB; gene aprB
SwissProt
Manually annotated by BRENDA team
Allochromatium vinosum D
strain D
-
-
Manually annotated by BRENDA team
Columbia ecotype
-
-
Manually annotated by BRENDA team
ecotype Columbia-0
-
-
Manually annotated by BRENDA team
var. columbia
-
-
Manually annotated by BRENDA team
archaebacterium
VC-16
-
-
Manually annotated by BRENDA team
archaebacterium VC-16
VC-16
-
-
Manually annotated by BRENDA team
O28603: adenylylsulfate reductase, O2860: subunit A adenylylsulfate reductase, subunit B
O28603 and O28604
SwissProt
Manually annotated by BRENDA team
Q59339: alpha-subunit, Q59338: beta-subunit
Q59339 and Q59338
SwissProt
Manually annotated by BRENDA team
subunit A and subunit B
O28603 and O28604
SwissProt
Manually annotated by BRENDA team
Archaeoglobus fulgidus ATCC 49558
subunit A and subunit B
O28603 and O28604
SwissProt
Manually annotated by BRENDA team
Astragalus crassicarpus
-
-
-
Manually annotated by BRENDA team
Astragalus tephrosioides
-
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
Burkholderia cepacia DBO1
DBO1
-
-
Manually annotated by BRENDA team
strain CM, genes aprA and aprB
-
-
Manually annotated by BRENDA team
Candidatus Ruthia magnifica CM
strain CM, genes aprA and aprB
-
-
Manually annotated by BRENDA team
aprA; gene aprA
UniProt
Manually annotated by BRENDA team
aprB; gene aprB
UniProt
Manually annotated by BRENDA team
strain TLS, genes aprA and aprB
-
-
Manually annotated by BRENDA team
Chlorobaculum tepidum TLS
strain TLS, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain CaD3, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain CaD3, genes aprA and aprB
-
-
Manually annotated by BRENDA team
aprA fragment; f.sp. thiosulfatophilum, strain DSM 245, gene aprA
UniProt
Manually annotated by BRENDA team
aprB fragment; f.sp. thiosulfatophilum, DSM 245, gene aprB
UniProt
Manually annotated by BRENDA team
strain BS1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
strain BS1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
Chromatium sp.
weak activity
-
-
Manually annotated by BRENDA team
strain MLMS-1
-
-
Manually annotated by BRENDA team
Desulfobulbus sp. MLMS-1
strain MLMS-1
-
-
Manually annotated by BRENDA team
strain 8395, strain 8351
-
-
Manually annotated by BRENDA team
strain DSM 12254
-
-
Manually annotated by BRENDA team
G100A, ATCC27774, API, ATCC 13541, Norway; weak activity
-
-
Manually annotated by BRENDA team
strain 8301 (Norway), strain 8307, strain 8380
-
-
Manually annotated by BRENDA team
strain ATCC 19364
-
-
Manually annotated by BRENDA team
alpha subunit and beta subunit; strain Miyazaki F
B8PS61 and B8DS74
UniProt
Manually annotated by BRENDA team
str. Hildenborough
Q72DT3
UniProt
Manually annotated by BRENDA team
strain 8303, strain 8305
-
-
Manually annotated by BRENDA team
strain Hildenborough
-
-
Manually annotated by BRENDA team
strain Marburg
-
-
Manually annotated by BRENDA team
strain Miyazaki
-
-
Manually annotated by BRENDA team
subsp. vulgaris, strain DSM 644, gene apsA
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough
str. Hildenborough
Q72DT3
UniProt
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough
strain Hildenborough
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Marburg
strain Marburg
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki
strain Miyazaki
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki F
alpha subunit and beta subunit; strain Miyazaki F
B8PS61 and B8DS74
UniProt
Manually annotated by BRENDA team
genes aprA and aprB
-
-
Manually annotated by BRENDA team
weak activity
-
-
Manually annotated by BRENDA team
aprA fragment; gene aprA
UniProt
Manually annotated by BRENDA team
aprB fragment; gene aprB
UniProt
Manually annotated by BRENDA team
Delta1 symbiont
UniProt
Manually annotated by BRENDA team
genes aprA and aprB
-
-
Manually annotated by BRENDA team
aprA; gene aprA
UniProt
Manually annotated by BRENDA team
aprB; gene aprB
UniProt
Manually annotated by BRENDA team
strain BU-1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
Pelodictyon clathratiforme BU-1
strain BU-1, genes aprA and aprB
-
-
Manually annotated by BRENDA team
f. sp. thiosulfatophilum
-
-
Manually annotated by BRENDA team
beta-subunit
A0LH39
UniProt
Manually annotated by BRENDA team
Tetraselmis sp.
-
-
-
Manually annotated by BRENDA team
alpha-subunit; ATCC 25259
UniProt
Manually annotated by BRENDA team
beta-subunit; ATCC 25259
UniProt
Manually annotated by BRENDA team
strain ATCC 25259, genes aprA and aprB
-
-
Manually annotated by BRENDA team
aprA fragment; gene aprA
UniProt
Manually annotated by BRENDA team
aprB fragment; gene aprB
UniProt
Manually annotated by BRENDA team
aprA fragment; gene aprA
UniProt
Manually annotated by BRENDA team
aprB fragment; gene aprB
UniProt
Manually annotated by BRENDA team
aprA fragment; gene aprA
UniProt
Manually annotated by BRENDA team
aprB fragment; gene aprB
UniProt
Manually annotated by BRENDA team
large subunit AprA and small subunit AprB
F6KEW4 and F6KEW3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
APS reductase is a key enzyme involved in the pathways of sulfate reduction and sulfide oxidation in the biological sulfur cycle
physiological function
-
key enzyme of the dissimilatory sulfate respiration
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-adenylylsulfate + dithioerythritol
adenosine 5'-monophosphate + sulfite + oxidized dithioerythritol
show the reaction diagram
-
-
-
-
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
show the reaction diagram
O81350, -
-
-
-
ir
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
O33996, O33997
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC0, A8JZC1
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC4, A8JZC5
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC6, A8JZC7
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC8, A8JZC9
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB8, A8JZB9, -
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB0, A8JZB1
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB6, A8JZB7
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
O33996, O33997
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC0, A8JZC1
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC4, A8JZC5
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC6, A8JZC7
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC8, A8JZC9
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB8, A8JZB9, -
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB0, A8JZB1
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB6, A8JZB7
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
the enzyme catalyzes the first committed step in bacterial sulfate reduction, conserved and semiconserved residues participate in four main-chain hydrogen bonds with adenine and the ribose O2'-hydroxyl, interaction between the phosphosulfate and APSR occurs via strictly conserved residues K144, R242, and R245, the phosphosulfate is also positioned opposite an [4Fe-4S] cofactor and Cys140. However, the substrate is not in direct contact with the [4Fe-4S] cluster, overview
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
Chlorobaculum tepidum TLS
-
-, APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-, APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
Candidatus Ruthia magnifica CM
-
-, APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-, APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
Pelodictyon clathratiforme BU-1
-
-, APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + dithioerythritol
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithioerythritol
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithioerythritol
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithioerythritol
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithioerythritol
AMP + sulfite + oxidized dithioerythritol
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithionite
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithionite
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + dithiothreitol
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + ferrocytochrome c3
AMP + sulfite + ferricytochrome
show the reaction diagram
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki
-
-
-
-
?
adenylyl sulfate + GSH
AMP + sulfite + GSSG
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + GSH
AMP + sulfite + GSSG
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + GSH
AMP + sulfite + GSSG
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
B8PS61 and B8DS74
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
O28603 and O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-, O28603
-
-
-
r
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
constitutive enzyme participates in oxidation of sulfite via the adenylyl sulfate pathway, that yields ATP through substrate-level phosphorylation
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in vectorial electron transport of cells grown on hydrogen plus sulfate as the sole energy source
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
key enzyme of assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
key enzyme of the dissimilatory sulfate respiration
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Archaeoglobus fulgidus ATCC 49558
O28603 and O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Desulfovibrio vulgaris Marburg
-
enzyme is involved in vectorial electron transport of cells grown on hydrogen plus sulfate as the sole energy source
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Allochromatium vinosum D
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Desulfovibrio vulgaris Miyazaki F
B8PS61 and B8DS74
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Burkholderia cepacia DBO1
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced glutaredoxin 1
AMP + sulfite + oxidized glutaredoxin 1
show the reaction diagram
-
can use 3'-phosphoadenylyl sulfate as sulfate donor
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin
AMP + sulfite + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin
AMP + sulfite + oxidized thioredoxin
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin 1
AMP + sulfite + oxidized thioredoxin 1
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin 1
AMP + sulfite + oxidized thioredoxin 1
show the reaction diagram
-
can use 3'-phosphoadenylyl sulfate as sulfate donor
-
-
?
adenylylsulfate + thioredoxin
AMP + sulfite + ?
show the reaction diagram
-
-
-
-
?
ADP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
-
-
-
?
ADP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
50% of the activity with AMP
-
-
?
AMP + sulfite + acceptor
adenylyl sulfate + reduced acceptor
show the reaction diagram
-, O28603
-
-
-
r
AMP + sulfite + acceptor
adenylyl sulfate + reduced acceptor
show the reaction diagram
Q59339 and Q59338
-
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
show the reaction diagram
-
-
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
show the reaction diagram
-
-
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
show the reaction diagram
-
-
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
show the reaction diagram
-
no activity with cytochrome c
-
-
-
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
show the reaction diagram
-
reaction with horse heart cytochrome c, no activity with cytochrome c from Candida krusei
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
-, O28603 and O28604
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium VC-16
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
-
-
-
?
AMP + sulfite + [Fe(CN)6]3-
adenylyl sulfate + [Fe(CN)6]4-
show the reaction diagram
F6KEW4 and F6KEW3
-
-
-
-
ATP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
24% of the activity with AMP
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
archaebacterium
-
24% of the activity with AMP
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
12.8% of the activity with AMP
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
archaebacterium VC-16
-
24% of the activity with AMP
-
-
?
CMP + sulfite + cytochrome c
cytidylyl sulfate + ?
show the reaction diagram
-
7% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
-
7.6% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium
-
24% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
-
8% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
-
no activity with CMP
-
-
-
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
-
41% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium VC-16
-
24% of the activity with AMP
-
-
?
dAMP + sulfite + cytochrome c
deoxyadenylyl sulfate + ?
show the reaction diagram
-
80% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
show the reaction diagram
-
128% of maximal activity
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
show the reaction diagram
-
82.7% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
show the reaction diagram
-
74% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium, archaebacterium VC-16
-
74% of the activity with AMP
-
-
?
GMP + sulfite + cytochrome c
guanylyl sulfate + ?
show the reaction diagram
-
-
-
-
?
GMP + sulfite + cytochrome c
guanylyl sulfate + ?
show the reaction diagram
-
9% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
68% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium
-
68% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
GMP is as active as AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
51% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
29.4% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
54% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
-
94% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
archaebacterium VC-16
-
68% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
show the reaction diagram
Allochromatium vinosum D
-
94% of the activity with AMP
-
-
?
guanylyl sulfate + reduced methyl viologen
GMP + methyl viologen + sulfite
show the reaction diagram
-
-
-
-
?
IMP + sulfite + cytochrome c
?
show the reaction diagram
-
62% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
-
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
archaebacterium
-
41% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
74% of the activity with AMP
-
-
?
UMP + sulfite + cytochrome c
uridylyl sulfate + ?
show the reaction diagram
-
9% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
-
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
7.6% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
8% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
33% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
no activity with UMP
-
-
-
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
-
36% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
show the reaction diagram
Allochromatium vinosum D
-
33% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
show the reaction diagram
-
90% of the activity with AMP
-
-
?
additional information
?
-
-
adenosine 5'-phosphosulfate sulfotransferase and adenosine 5'-phosphosulfate reductase are identical enzymes
-
-
-
additional information
?
-
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
O33996
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
Q72DT3
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
Q9L768
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
B5QSJ0
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
A0LH39
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
Q5VLA6, Q5VLA7
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
Q8KE28
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
Desulfovibrio vulgaris Hildenborough
Q72DT3
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
additional information
?
-
Desulfobulbus sp. MLMS-1
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
O33996, O33997
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC0, A8JZC1
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC4, A8JZC5
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC6, A8JZC7
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZC8, A8JZC9
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB8, A8JZB9, -
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB0, A8JZB1
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
A8JZB6, A8JZB7
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
-
the enzyme catalyzes the first committed step in bacterial sulfate reduction
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
show the reaction diagram
Chlorobaculum tepidum TLS, Chlorobium chlorochromatii CaD3, Candidatus Ruthia magnifica CM, Chlorobium phaeobacteroides BS1, Pelodictyon clathratiforme BU-1
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
O28603 and O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
constitutive enzyme participates in oxidation of sulfite via the adenylyl sulfate pathway, that yields ATP through substrate-level phosphorylation
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in vectorial electron transport of cells grown on hydrogen plus sulfate as the sole energy source
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
key enzyme of assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
key enzyme of the dissimilatory sulfate respiration
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Archaeoglobus fulgidus ATCC 49558
O28603 and O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Desulfovibrio vulgaris Marburg
-
enzyme is involved in vectorial electron transport of cells grown on hydrogen plus sulfate as the sole energy source
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Allochromatium vinosum D
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Burkholderia cepacia DBO1
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
Desulfovibrio vulgaris Hildenborough
-
key step in sulfur cycle
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4Fe-4S-center
B8PS61 and B8DS74
contains two 4Fe-4S clusters in the beta-subunit
dihydroriboflavin
-
can donate electrons directly to adenylyl sulfate reductase
FAD
-
enzyme contains 0.74 mol of FAD per mol of enzyme
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
archaebacterium
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
O28603
flavoenzyme.The two electrons required for adenylyl sulfate reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
contains 1.4 mol of FAD per mol of enzyme
FAD
-
enzyme contains FAD
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
located nearby Fe-S center I, pointing ist C-8 methyl group to the iron-sulfur center
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme; noncovalently bound
FAD
-
electron mediator
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
-
enzyme contains 1 mol of FAD per mol of enzyme
FAD
B8PS61 and B8DS74
contains a noncovalently bound FAD
FAD
-
FAD is noncovalently attached to the alpha-subunit
FAD
-, O28603 and O28604
FAD-containing alpha-subunit
FADH2
-
can donate electrons directly to adenylyl sulfate reductase
flavin
-
contains 1 mol of flavin per mol of enzyme
flavin
O28603
flavoenzyme
flavin
-
flavin is absent
FMNH2
-
can donate electrons directly to adenylyl sulfate reductase
heme
-
contains 2 heme groups of cytochrome c characterper mol of enzyme
iron-sulfur centre
-
two [4Fe-4S] clusters are enveloped by cluster-binding motifs
additional information
-
the enzyme contains a [4Fe-4S] cluster cofactor
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4Fe-4S cluster
O28603
flavoenzyme.The two electrons required for adenylyl sulfate reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD. The large difference in reduction potential of these clusters (-60 mV and -500 mV) can be explained by interactions of the clusters with the protein matrix
Fe2+
-
the enzyme contains a [4Fe-4S] cluster cofactor
Iron
-
contains 6-8 gatom of nonheme iron
Iron
-
contains 6-11 gatom of nonheme iron
Iron
-
contains 8-10 gatom of nonheme iron
Iron
-
contains 4 gatom of nonheme iron and 2 gatom of heme iron
Iron
-
enzyme contains 6.3 mol iron per mol of enzyme
Iron
-
iron sulfur protein, contains 8 iron atoms per 93000 Da protein, two [4Fe-4S] clusters
Iron
-
enzyme contains 6-11 non-heme Fe per mol
Iron
-
contains 8 mol of iron per mol of enzyme
Iron
-
contains 4-6 mol of non-haem iron per mol of enzyme
Iron
O28603
the two electrons required for the adenylyl sulfate reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD
Iron
-
enzyme contains 12.7 mol of iron per 22000 Da enzyme
Iron
-
contains nonheme iron
Iron
-
contains nonheme iron
Iron
-
contains 4 mol of non-heme iron per mol of enzyme
Iron
-
contains 7 mol of Fe per mol of enzyme
Iron
-
4 paramagnetic iron sites, which form a diamagnetic [4Fe-4S]2+ cluster
Iron
-
two [4Fe-4S] clusters, one cluster is deeply buried in the protein matrix, Fe-S center I, center II is located at the surface of the protein
Iron
-
contains 5.6 iron per alpha,beta heterodimer, novel Fe-S structure, possibly with an iron-nuclearity greater than four
Iron
-
contains a [4Fe-4S] cluster
Iron
-
contains 8 mol of nonheme iron per mol of enzyme
Iron
-
contains 8-13 mol of non-heme iron per mol of enzyme
Iron
-
contains 8-10 mol of non-heme iron per mol of enzyme
Iron
-
Cys139, Cys228 and Cys231 act as ligands to a [3Fe-4S] cluster
Iron
-
contains a cubane 4Fe-4S cluster
Iron
O33996
contains two [4Fe-4S] centers
Iron
-
contains two [4Fe-4S] centers
Iron
Q8KE28
contains two [4Fe-4S] centers
Iron
Q9L768
contains two [4Fe-4S] centers
Iron
Q72DT3
contains two [4Fe-4S] centers
Iron
B5QSJ0
contains two [4Fe-4S] centers
Iron
-
contains two [4Fe-4S] centers
Iron
A0LH39
contains two [4Fe-4S] centers
Iron
Q5VLA6, Q5VLA7
contains two [4Fe-4S] centers; contains two [4Fe-4S] centers
Iron-sulfur cluster
-, O28603 and O28604
beta-subunit harbours two [4Fe-4S] clusters
Iron-sulfur cluster
Q59339 and Q59338
-
iron-sulfur clusters
-
iron-sulfur flavoprotein containing two distinct [4Fe-4S] dusters
additional information
-
stimulation by high ionic strength
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-[2-(1,2-dicarboxyethylamino)ethylamino]butanedioic acid
O28603 and O28604
-
-
2-[2-[bis(carboxymethyl)amino]ethyl-(2-hydroxymethyl)amino]acetic acid
O28603 and O28604
-
-
3'-phosphoadenosine-5'-phosphate
-
-
AMP
-
inhibits reaction with cytochrome c above 0.1 mM, inhibits reaction with ferricyanide above 1.6 mM
cysteine
-
1 mM, significant inhibition
EDTA
O28603 and O28604
-
iodoacetamide
-
5 mM, 54% inhibition
NaN3
-
10 mM, no loss of the activity with ferricyanide, 52% loss of the activity with cytochrome c
NEM
-
5 mM, 49% inhibition
NEM
-
10 mM, 45% loss of activity with ferricyanide, complete loss of activity with cytochrome c
NEM
-
10 mM, complete inhibition
NEM
-
5 mM complete inhibition
PCMB
-
1 mM, 30% inhibition
PCMB
-
1 mM, 23% loss of the activity with ferricyanide, complete loss of activity with cytochrome c
PCMB
-
0.1 mM, 30% inhibition
PCMB
-
1 mM, complete inhibition
potassium phosphate
-
inhibits reaction with cytochrome c
Sodium arsenite
-
10 mM, no loss of the activity with ferricyanide, 88% loss of the activity with cytochrome c
iodoacetamide
-
10 mM 2% loss of the activity with ferricyanide, 19% loss of the activity with cytochrome c
additional information
-
inhibitor binding structure, binding energies, dissociation constants, and inhibition mechanisms, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
buthionine sulfoximine
-
1 mM, 2fold stimulation of activity
menadione
-
stimulates oxidation of ferrocytochrome c3 with adenylyl sulfate and FAD as electron mediator
Na2SO4
O81350, -
100 mM
Na2SO4
-
500 mM, 5 fold stimulation
NaCl
-
APR activity of all three isoforms increases 3fold in roots after 5 h of treatment with 150 mM NaCl
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.011
-
5'-adenylylsulfate
-
-
0.0065
-
adenylyl sulfate
-
-
0.015
-
adenylyl sulfate
-
-
0.019
-
adenylyl sulfate
-
-
0.029
-
adenylyl sulfate
-
pH 8 and saturating thioredoxin 1
0.105
-
adenylyl sulfate
-
pH 8 and saturating glutaredoxin 1
0.25
-
adenylyl sulfate
-
-
0.0025
-
AMP
-
reaction with cytochrome c
0.041
-
AMP
-
reaction with ferricyanide
0.05
-
AMP
-
reaction with cytochrome c
0.09
-
AMP
-
reaction with ferricyanide
0.091
-
AMP
-
reaction with cytochrome c
0.1
-
AMP
-
reaction with ferricyanide
0.18
-
AMP
-
reaction with cytochrome c
0.3
-
AMP
-
reaction with ferricyanide
1
-
AMP
archaebacterium
-
-
3.1
-
CMP
-
reaction with cytochrome c
0.021
-
cytochrome c
-
-
0.033
-
cytochrome c
-
-
0.0002
-
dithiothreitol
-
-
0.089
-
ferricyanide
-
-
0.091
-
ferricyanide
-
-
0.13
-
ferricyanide
-
-
0.16
-
ferricyanide
-
-
0.16
-
ferricyanide
-
-
0.4
-
ferricyanide
archaebacterium
-
-
0.022
-
glutaredoxin 1
-
pH 8 and saturating adenylyl sulfate
-
0.01
-
GMP
-
reaction with cytochrome c
0.63
-
GMP
-
reaction with ferricyanide
1.25
-
GMP
-
reaction with cytochrome c
3
-
GMP
-
reaction with ferricyanide
0.025
-
guanylyl sulfate
-
-
0.8
-
IMP
-
reaction with ferricyanide
1.5
-
IMP
-
reaction with cytochrome c
0.015
-
riboflavin
-
-
0.017
-
sulfite
-
reaction with cytochrome c
0.071
-
sulfite
-
reaction with cytochrome c
0.073
-
sulfite
-
reaction with ferricyanide
0.093
-
sulfite
-
reaction with cytochrome c
0.91
-
sulfite
-
-
1.3
-
sulfite
-
reaction with ferricyanide
1.5
-
sulfite
-
reaction with ferricyanide
1.5
-
sulfite
-
reaction with ferricyanide
2.5
-
sulfite
-
reaction with ferricyanide
2.7
-
thioredoxin
-
thioredoxin originating from Clamydomonas reinhardtii
8.6
-
thioredoxin
-
thioredoxin originating from Escherichia coli
0.053
-
thioredoxin 1
-
pH 8 and saturating adenylyl sulfate
4.5
-
UMP
-
reaction with cytochrome c
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0001
-
Astragalus crassicarpus
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0003
-
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0005
-
Astragalus crotalariae, Astragalus tephrosioides
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0006
-
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0013
-
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.0017
-
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30C for 30 min
0.011
-
O81350, -
mutant enzyme 342S
0.15
-
O81350, -
mutant enzyme 345S
0.302
-
-
mutant enzyme C140S, at 30C in 100 mM Tris-HCl buffer pH 8.0 containing 1 mM EDTA, 5 mM DTT, 0.106 mM thioredoxin from Escherichia coli, and 0.05 mM APS
2.39
-
archaebacterium
-
-
3.5
-
O81350, -
mutant enzyme C250S
4.6
-
-
untagged APS reductase using Escherichia coli thioredoxin
5.1
-
-
His-tagged APS reductase using Escherichia coli thioredoxin
7.248
-
O81350, -
wild type enzyme
10.3
-
-
wild type enzyme, at 30C in 100 mM Tris-HCl buffer pH 8.0 containing 1 mM EDTA, 5 mM DTT, 0.106 mM thioredoxin from Escherichia coli, and 0.05 mM APS
30
40
-
-
additional information
-
-
specificity runs though a maximum after 30 h of growth
additional information
-
-
-
additional information
-
-
-
additional information
-
-
L-cysteine and glutathione reduce the enzyme activity both in vitro and in vivo
additional information
-
-
specific activities in transgenic Arabidopsis thaliana shoots transfected with Pseudomonas aeruginosa adenylyl-sulfate reductase
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
-
oxidation of methyl viologen
7
-
-
ferricyanide assay, phosphate buffer
7.2
-
-
reaction with AMP, SO32- and ferricyanide
7.4
-
-
reaction with AMP, SO32- and ferricyanide
7.4
-
-
ferricyanide assay, Tris-HCl buffer
7.5
-
-
reaction with cytochrome c and UMP or CMP
7.6
-
-, O28603 and O28604
assay at
7.7
-
-
reaction with ferricyanide
8
-
-
reaction with AMP, SO32- and ferricyanide
8
-
archaebacterium
-
-
8
-
-
reaction with ferricyanide
8.5
-
-
reaction with adenylyl sulfate and dithiothreitol
8.8
-
-
reaction with cytochrome c
9
-
-
reaction with AMP, SO32- and cytochrome c
9
-
-
reaction with cytochrome c and IMP or GMP
9
-
-
reaction with cytochrome c
9.5
-
-
reaction with AMP, SO32- and cytochrome c
9.5
-
-
reaction with cytochrome c and AMP
9.5
-
-
reaction with cytochrome c as electron acceptor, Tris-HCl buffer
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
85
-
archaebacterium
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70
90
archaebacterium
-
70C: about 65% of maximal activity, 90C: about 90% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
axenic cell suspension culture
Manually annotated by BRENDA team
-
3fold decline in activity during development can be attributed to a reduction of enzyme during aging of individual leaves, the highest activity occurs in the youngest leaves and the lowest in fully expanded leaves
Manually annotated by BRENDA team
-
APS reductase enhances strongly in the shoots of sulfate-deprived plants, and rapidly decreases again upon sulfate re-supply
Manually annotated by BRENDA team
additional information
-
extracts of sulfite-grown cells have lower activity than extracts of sulfate-grown cells
Manually annotated by BRENDA team
additional information
Desulfovibrio vulgaris Miyazaki
-
extracts of sulfite-grown cells have lower activity than extracts of sulfate-grown cells
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
exclusively located in chloroplast
Manually annotated by BRENDA team
Allochromatium vinosum D
-
-
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough
-
-
-
Manually annotated by BRENDA team
-
87% of the activity is located on the cytoplasmic side of the cytoplasmic membrane
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Marburg
-
87% of the activity is located on the cytoplasmic side of the cytoplasmic membrane
-
-
Manually annotated by BRENDA team
additional information
-
mitochondrial or cytoplasmic localization
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
calculated from sequence of cDNA, C-terminal domain of EiAPR; MALDI-TOF mass spectrometry, C-terminal domain of EiAPR
28350
-
-
calculated average mass, determined on the elemental composition of the apoprotein plus the components in the metal center, assuming that all cysteines are in reduced form and the metal cluster has an oxidation state of zero
28360
-
-
calculated from amino acid sequence
28560
-
-
calculated from amino acid sequence
28700
-
-
gel filtration
28710
-
-
electrospray FT-ICR mass spectrometry
28710
-
-
ESI-FTICR mass spectrometry; theoretical value based on the chemical formula
30470
-
-
MALDI-TOF mass spectrometry, the enzyme used is a recombinant protein with 48 additional residues containing the His6 tag
35000
-
-
SDS-PAGE
35430
-
-
mass spectrometry
48000
-
O81350, -
non-reducing and reducing SDS-PAGE
48700
-
-
MALDI-TOF mass spectrometry, whole enzyme
48710
-
-
calculated from sequence of cDNA, whole enzyme
52000
-
-
SDS-PAGE
90000
124000
-
dynamic light scattering
96000
-
O81350, -
non-reducing SDS-PAGE, 16% of the protein was present as a homodimer
160000
-
archaebacterium
-
gel filtration
160000
-
-
gel filtration
175000
-
-
gel filtration
180000
-
-
gel filtration
186000
-
-
smallest catalytic active subunit, also aggregations of 324000 Da and 569000 Da are detected, gel filtration
190000
-
-
gel filtration
200000
-
-
estimation from sedimentation coefficient
210000
-
-
gel filtration
400000
-
-
gel filtration
439500
-
-
equilibrium sedimentation
600000
-
-
gel filtration, the majority of the protein is aggregated
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 70000 + x * 26000, SDS-PAGE
?
-
x * 70000 + x * 26000, SDS-PAGE
?
-
x * 72000 + x * 20000, SDS-PAGE
?
-
x * 52000, SDS-PAGE
?
-
x * 28000, SDS-PAGE
dimer
archaebacterium
-
2 * 80000, SDS-PAGE
dimer
-
alpha,beta, 1 * 75000 + 1 * 20000, SDS-PAGE
dimer
archaebacterium VC-16
-
2 * 80000, SDS-PAGE
-
heterodimer
-
1 * 18000 + 1 * 75000, containing one FAD per molecule and eight iron atoms arranged in two [4Fe-4S] clusters, SDS-PAGE
heterodimer
B8PS61 and B8DS74
1 * 75000 + 1 * ?, X-ray crystallography
heterodimer
-
functional enzyme
heterodimer
F6KEW4 and F6KEW3
1 * 70000 + 1 * 20000, SDS-PAGE (in denaturing gels, only the small subunit is visible because the large AprA subunit probably overlapped with the highly abundant a-subunit of reverse methylcoenzyme M reductase)
heterodimer
Desulfovibrio vulgaris Miyazaki F
-
1 * 75000 + 1 * ?, X-ray crystallography
-
heterohexamer
-
non-functional protein
heterotetramer
-
1 * 75000 + 1 * 20000, alpha2beta2 heterotetramer
hexamer
-
APSR comprises six alphabeta-heterodimers that form a hexameric structure, X-ray crystallography
homodimer
-
2 * 27000, SDS-PAGE
homodimer
O81350, -
2 * 48000, non-reducing SDS-PAGE, 16% of the protein is present as a homodimer
monomer
-
1 * 35000, SDS-PAGE, a homodimer can be formed in solution depending on the redox potential
monomer
O81350, -
1 * 48000, non-reducing and reducing SDS-PAGE
monomer
-
SDS-PAGE
monomer
Q9ZP23
SDS-PAGE
monomer
-
1 * 28700, ESI-FTICR mass spectrometry
monomer
-
1 * 28513, analytical ultracentrifugation
oligomer
Q59339 and Q59338
2 * 80000 + 1 * 18500, alpha2beta structure, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 67800 + 2 * 25600, smallest catalytic active unit, SDS-PAGE
tetramer
-
alpha2beta2, 2 * 73300 + 2 * 17100, SDS-PAGE
tetramer
Desulfovibrio vulgaris Hildenborough
-
alpha2beta2, 2 * 67800 + 2 * 25600, smallest catalytic active unit, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; the structures of the enzyme in the two-electron reduced state and with sulfite bound to FAD are reported at 1.6 A and 2.5 A resolution, respectively
O28603
hanging-drop vapour-diffusion method using PEG 4000 as precipitant. Crystals grow in space group P2(1)2(1)2(1), with unit-cell parameters a = 72.4, b = 113.2, c = 194.0 A. The asymmetric unit probably contains two units. The crystals diffract beyond 2 A resolution and are suitable for X-ray structure analysis
-, O28603 and O28604
dynamic light scattering, ultracentrifugation, and electron paramagnetic resonance methods
-
hanging drop vapor diffusion method, using 20% (w/v) PEG 6000 and 60 mM ammonium sulfate in Tris buffer (0.1 M, pH 7.0), at 18C
-
hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 0.1 M NaCl, 2.0 M ammonium sulfate and 15% (v/v) glycerol, at 4C
B8PS61 and B8DS74
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
2 h, more than 30% loss of activity
60
-
-
1 h, stable
60
-
-
heating for longer periods results in protein precipitation with simultaneous loss of activity
60
-
-
6 min, stable
65
-
-
5 min, complete loss of activity
70
-
-
2 min, 50% loss of activity
75
-
-
thermotolerant up to
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable to air with a half-life of 12 min, the 4Fe-4S cluster is converted into a 2Fe-2S form
-
30-50% loss of activity by repeated freezing and thawing
-
enzyme is rapidly denatured by even micromolar concentrations of ferricyanide
-
total enzyme activity is significantly decreased by ammonium sulfate precipitation, leaving 20% of the initial activity in the supernatant
F6KEW4 and F6KEW3
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxygen causes complete loss of activity
-
659441
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, continous loss of activity, precipitation after 2-3 days
-
-20C, stable for several weeks
-
4C, more than 2 days, more than 30% loss of activity
-
-18C, 88-90% loss of activity after 1 week, 68% loss of activity after 16 days, in presence of 50% glycerol, 46% loss of activity after 16 days
-
4C, more than 20% loss of activity after 8 h
-
-20C, much loss of activity after 30 days
-
4C, continous loss of activity
-
frozen, protein concentration above 5 mg/ml, stable for several months
-
5C, 5 days, 20% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
archaebacterium
-
isolated under the exclusion of oxygen
-, O28603 and O28604
purification of a recombinant tagged protein by chitin affinity chromatography
-
DEAE-Biogel A chromatography, Source 15 column chromatography, and Superdex 200 column chromatography
-
DE-52 column chromatography, macro-DEAE column chromatography, and hydroxyapatite column chromatography
-
DEAE-Toyopearl 650S column chromatography, Sephacryl S-200 gel filtration, and Superdex 200 gel filtration
B8PS61 and B8DS74
HiTrap chelating column chromatography
-
purification of a recombinant His-tagged protein and several mutants by Ni2+ affinity chromatography
-
Ni2+ affinity chromatography
O81350, -
Ni2+-affinity column chromatography
-
partial purification by ammonium sulfate precipitation and Q-Sepharose column chromatography
F6KEW4 and F6KEW3
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expressed in Eschericha coli as the N-terminal reductase domain (AcAPR1-N) and the C-terminal glutaredoxin domain (AcAPR1-C). Recombinant full-length ATP sulfurylase (AcATPS1) and recombinant full length adenosine-5'-phosphosulfate reductase (AcAPR1) from Allium cepa can form a physical association
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
O33996
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
O33996, O33997
overexpression in Escherichia coli
-
overexpression of a His-tagged recombinant protein in Escherichia coli
-
-
Q59339 and Q59338
expression in Escherichia coli of a tagged recombinant protein
-
expressed in Escherichia coli
Q9ZP23
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
expression in Escherichia coli
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZB6, A8JZB7
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
Q8KE28
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZB0, A8JZB1
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
Q9L768
expressed in Escherichia coli JM109 cells
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
Q72DT3
gene apsA, PCR-based DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZC4, A8JZC5
overexpression in Escherichia coli
-
expressed in Escherichia coli
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
B5QSJ0
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZB8, A8JZB9, -
expressed in Escherichia coli
-
expressed in Zea mays
-
expression in Escherichia coli of a recombinant His-tagged protein and several mutants
-
localized expression in plastids of Arabidopsis thaliana, transgenic plants accumulate sulfite, thiosulfate, cysteine and gluthatione
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
A0LH39
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation; full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
Q5VLA6, Q5VLA7
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZC0, A8JZC1
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZC8, A8JZC9
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview; genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
A8JZC6, A8JZC7
expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APR mRNA levels of all three isoforms increase 3fold in roots after 5 h of treatment with 150 mM NaCl. In mutants deficient in cytokinin and auxin, jasmonate, salicylate, or ethylene signaling APR mRNA levels are increased upon salt exposure similar to wild type plants, however, APR enzyme activity is not affected by salt in these plants. Signaling via gibberellic acid is essential for the increase in APR mRNA by salt treatment. Addition of 0.1 mM salicylate to the nutrient solution leads to an increase of mRNA levels of all three APR isoforms. 0.2 mM 1-aminocyclopropane carboxylic acid and 0.045 mM jasmonate increase accumulation of APR1 and APR3 transcripts, but do not affect the APR2 isoform.
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C139S
Q9ZP23
no detectable activity
C140S
Q9ZP23
reduced activity compared to wild type enzyme
C228S
Q9ZP23
reduced activity compared to wild type enzyme
C231S
Q9ZP23
reduced activity compared to wild type enzyme
C256S
Q9ZP23
reduced activity compared to wild type enzyme
C129S
-
maximal velocity dropps to 50% of that of the wild-type enzyme
C248S
-
mutation completely abolishes enzyme activity
C140S
-
the mutation has a deleterious effect on the amount of iron associated with the enzyme, no detectable catalytic activity
C141S
-
the mutation has a deleterious effect on the amount of iron associated with the enzyme, no detectable catalytic activity
C223S
-
the mutation has a deleterious effect on the amount of iron associated with the enzyme, no detectable catalytic activity
C226S
-
the mutation has a deleterious effect on the amount of iron associated with the enzyme, no detectable catalytic activity
C249S
-
the mutation has a deleterious effect on the amount of iron associated with the enzyme, no detectable catalytic activity
C249S
-
unreactive toward 4-vinylpyridine labelling
C59S
-
the mutation has a deleterious effect on the amount of iron associated with the enzyme, low catalytic activity
C59S
-
unreactive toward 4-vinylpyridine labelling
C139S
-
inactive mutant with no iron present
C139S
-
no detectable activity
C140S
-
catalytic iron content is retained, but the mutant is inactive
C140S
-
3% activity of the wild type enzyme
C228S
-
inactive mutant with no iron present
C228S
-
no detectable activity
C231S
-
inactive mutant with no iron present
C231S
-
no detectable activity
C256S
-
catalytic iron content is retained, but the mutant is inactive
C256S
-
no detectable activity
C165S
O81350, -
reduced activity compared to wild type enzyme
C166S
O81350, -
reduced activity compared to wild type enzyme
C250S
O81350, -
reduced activity compared to wild type enzyme
C257S
O81350, -
reduced activity compared to wild type enzyme
C260S
O81350, -
reduced activity compared to wild type enzyme
C285S
O81350, -
reduced activity compared to wild type enzyme
C342S
O81350, -
reduced activity compared to wild type enzyme
C345S
O81350, -
reduced activity compared to wild type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the inactive 2Fe-2S form can be converted into the 4Fe-4S form by adding an iron-sulfur cluster synthesizing-protein from Synechocystis, restoring the activity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
the gene apsA is used for quantitative determination of the organism in wastewater, overview
environmental protection
-
the gene apsA is used for quantitative determination of the organism in wastewater, overview
synthesis
-
production of adenosine 5'-phosphosulfate labeled with either 14C or 35S