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Information on EC 1.8.99.2 - adenylyl-sulfate reductase
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1.8.99.2 adenylyl-sulfate reductaseIUBMB Comments
An iron flavoprotein (FAD). Methylviologen can act as acceptor.
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Word Map
- 1.8.99.2
-
resection
-
abdominoperineal
- rectal
-
postoperative
-
anal
- women
-
excision
-
acute-phase
-
preoperative
-
perineal
-
pelvic
- rust
-
radiotherapy
-
curative
-
c-reactive
-
5-year
-
oncologic
-
laparoscopic
- puccinia
-
sphincter
-
anorectal
-
demographic
-
colostomy
- tritici
-
chemoradiotherapy
-
chemoradiation
-
verge
-
circumferential
-
anastomosis
- flap
- haptoglobin
-
intraoperative
-
ontario
-
neoadjuvant
-
dehiscence
-
stoma
-
actuarial
-
mesorectal
- incontinence
-
poisson
-
hernia
-
zoledronic
-
eortc
-
levator
-
psycinfo
- environmental protection
- synthesis
- analysis
- agriculture
-
ileostomy
-
race-specific
-
abdominis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
5'-adenylyl sulfate reductase, 5'-adenylylsulfate reductase, 5-adenylylsulfate reductase, AcAPR1, adenosine 5'-phosphosulfate reductase, adenosine phosphosulfate reductase, adenosine-5'-phosphosulfate reductase, adenylyl sulfate reductase, adenylylsulfate reductase, adenylylsulphate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-phosphosulfate reductase
adenosine phosphosulfate reductase
-
-
-
-
adenosine-5'-phosphosulfate reductase
adenylylsulfate reductase
AdoPSO4 reductase
-
-
-
-
AMP,sulfite:flavin oxidoreductase
-
-
-
-
APR
AprA
AprBA
APS reductase
APS-reductase
-
-
-
-
APSR
Dde_1110
dissimilatory APS reductase
dissimilatory APS reductases
EiAPR
reductase, adenylylsulfate
-
-
-
-
adenosine 5'-phosphosulfate reductase
-
-
-
-
adenosine-5'-phosphosulfate reductase
F6KEW4; F6KEW3
-
APS reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
-
-
-
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
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
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
mechanism
-
AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor
mechanism
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
reduction
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming)
An iron flavoprotein (FAD). Methylviologen can act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
9027-75-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-adenylylsulfate + dithioerythritol
adenosine 5'-monophosphate + sulfite + oxidized dithioerythritol
-
-
-
-
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
adenylyl sulfate + dithioerythritol
AMP + sulfite + oxidized dithioerythritol
-
-
-
-
?
adenylyl sulfate + reduced glutaredoxin 1
AMP + sulfite + oxidized glutaredoxin 1
-
can use 3'-phosphoadenylyl sulfate as sulfate donor
-
-
?
AMP + sulfite + [Fe(CN)6]3-
adenylyl sulfate + [Fe(CN)6]4-
F6KEW4; F6KEW3
-
-
-
-
CMP + sulfite + cytochrome c
cytidylyl sulfate + ?
-
7% of the activity with AMP
-
-
?
dAMP + sulfite + cytochrome c
deoxyadenylyl sulfate + ?
-
80% of the activity with AMP
-
-
?
guanylyl sulfate + reduced methyl viologen
GMP + methyl viologen + sulfite
-
-
-
-
?
UMP + sulfite + cytochrome c
uridylyl sulfate + ?
-
9% of the activity with AMP
-
-
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
-
-
-
-
?
5'-adenylylsulfate + dithiothreitol
adenosine 5'-monophosphate + sulfite + oxidized dithiothreitol
-
-
-
ir
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZC4, A8JZC5
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
the enzyme catalyzes the first committed step in bacterial sulfate reduction
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
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
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZB8, A8JZB9
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZC8, A8JZC9
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + ferrocytochrome c3
AMP + sulfite + ferricytochrome
-
-
-
-
?
adenylyl sulfate + ferrocytochrome c3
AMP + sulfite + ferricytochrome
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
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
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
O28603; O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
O28603
-
-
-
r
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key enzyme of the dissimilatory sulfate respiration
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
O28603; O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
Burkholderia cepacia DBO1 / ATCC 29424
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
Chromatium sp.
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
-
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
B8PS61; B8DS74
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
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
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
Desulfovibrio vulgaris Marburg / DSM 2119
-
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
B8PS61; B8DS74
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key enzyme of assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
Chromatium sp.
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced methyl viologen
AMP + sulfite + methyl viologen
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin
AMP + sulfite + oxidized thioredoxin
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin
AMP + sulfite + oxidized thioredoxin
-
-
-
-
?
adenylyl sulfate + reduced thioredoxin 1
AMP + sulfite + oxidized thioredoxin 1
-
can use 3'-phosphoadenylyl sulfate as sulfate donor
-
-
?
adenylyl sulfate + reduced thioredoxin 1
AMP + sulfite + oxidized thioredoxin 1
-
-
-
-
?
ADP + sulfite + ferricyanide
? + ferrocyanide
-
50% of the activity with AMP
-
-
?
AMP + sulfite + acceptor
adenylyl sulfate + reduced acceptor
O28603
-
-
-
r
AMP + sulfite + acceptor
adenylyl sulfate + reduced acceptor
-
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
-
no activity with cytochrome c
-
-
-
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
-
reaction with horse heart cytochrome c, no activity with cytochrome c from Candida krusei
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
-
-
-
-
?
AMP + sulfite + cytochrome c
adenylyl sulfate + ?
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
O28603; O28604
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
AMP + sulfite + ferricyanide
adenylyl sulfate + ferrocyanide
-
-
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
archaebacterium
-
24% of the activity with AMP
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
archaebacterium VC-16
-
24% of the activity with AMP
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
-
24% of the activity with AMP
-
-
?
ATP + sulfite + ferricyanide
? + ferrocyanide
-
12.8% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
archaebacterium
-
24% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
archaebacterium VC-16
-
24% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
-
7.6% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
-
41% of the activity with AMP
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
-
-
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
-
no activity with CMP
-
-
-
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
-
-
-
-
?
CMP + sulfite + ferricyanide
cytidylyl sulfate + ferrocyanide
-
8% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
archaebacterium
-
74% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
archaebacterium VC-16
-
74% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
-
74% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
-
82.7% of the activity with AMP
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
-
-
-
-
?
deoxyAMP + sulfite + ferricyanide
deoxyadenylyl sulfate + ferrocyanide
-
128% of maximal activity
-
-
?
GMP + sulfite + cytochrome c
guanylyl sulfate + ?
-
9% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
94% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
94% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
archaebacterium
-
68% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
archaebacterium VC-16
-
68% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
68% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
29.4% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
GMP is as active as AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
-
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
54% of the activity with AMP
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
-
-
-
?
GMP + sulfite + ferricyanide
guanylyl sulfate + ferrocyanide
-
51% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
archaebacterium
-
41% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
-
74% of the activity with AMP
-
-
?
IMP + sulfite + ferricyanide
? + ferrocyanide
-
90% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
33% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
33% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
7.6% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
36% of the activity with AMP
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
-
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
no activity with UMP
-
-
-
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
-
-
-
?
UMP + sulfite + ferricyanide
uridylyl sulfate + ferrocyanide
-
8% of the activity with AMP
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
-
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
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
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
O33996, O33997
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZB6, A8JZB7
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZB0, A8JZB1
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
-
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZC4, A8JZC5
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
the enzyme catalyzes the first committed step in bacterial sulfate reduction
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZB8, A8JZB9
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
-
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZC0, A8JZC1
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZC8, A8JZC9
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + cofactor sulfide
AMP + sulfite + cofactor disulfide
A8JZC6, A8JZC7
APS reductase is a key enzyme of the dissimilatory sulfate-reduction pathway
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
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
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
the enzyme is preferably required during the most rapid phase of growth
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
O28603 and O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key enzyme of the dissimilatory sulfate respiration
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
O28603 and O28604
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
Burkholderia cepacia DBO1 / ATCC 29424
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
Chromatium sp.
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme is involved in dissimilatory sulfate reduction
-
-
-
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
-
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
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
-
enzyme is involved in dissimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
Desulfovibrio vulgaris Marburg / DSM 2119
-
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
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key enzyme of assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
assimilatory sulfate reduction
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
key step in sulfur cycle
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
-
enzyme reduces adenylyl sulfate that is formed during dissimilatory reduction of sulfate
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dihydroriboflavin
-
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
-
4Fe-4S-center
B8PS61; B8DS74
contains two 4Fe-4S clusters in the beta-subunit
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
-
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
-
enzyme contains 1 mol of FAD per mol of enzyme
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METALS and IONS
ORGANISM
UNIPROT
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
Iron
Iron-sulfur cluster
iron-sulfur clusters
-
iron-sulfur flavoprotein containing two distinct [4Fe-4S] dusters
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
-
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
-
iron sulfur protein, contains 8 iron atoms per 93000 Da protein, two [4Fe-4S] clusters
Iron
-
contains 5.6 iron per alpha,beta heterodimer, novel Fe-S structure, possibly with an iron-nuclearity greater than four
Iron-sulfur cluster
O28603; O28604
beta-subunit harbours two [4Fe-4S] clusters
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[2-(1,2-dicarboxyethylamino)ethylamino]butanedioic acid
O28603; O28604
-
2-[2-[bis(carboxymethyl)amino]ethyl-(2-hydroxymethyl)amino]acetic acid
O28603; O28604
-
NaN3
-
10 mM, no loss of the activity with ferricyanide, 52% loss of the activity with cytochrome c
sodium arsenite
-
10 mM, no loss of the activity with ferricyanide, 88% loss of the activity with cytochrome c
additional information
-
inhibitor binding structure, binding energies, dissociation constants, and inhibition mechanisms, overview
-
AMP
-
inhibits reaction with cytochrome c above 0.1 mM, inhibits reaction with ferricyanide above 1.6 mM
iodoacetamide
-
10 mM 2% loss of the activity with ferricyanide, 19% loss of the activity with cytochrome c
NEM
-
10 mM, 45% loss of activity with ferricyanide, complete loss of activity with cytochrome c
PCMB
-
1 mM, 23% loss of the activity with ferricyanide, complete loss of activity with cytochrome c
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
menadione
-
stimulates oxidation of ferrocytochrome c3 with adenylyl sulfate and FAD as electron mediator
NaCl
-
APR activity of all three isoforms increases 3fold in roots after 5 h of treatment with 150 mM NaCl
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.7
thioredoxin
-
thioredoxin originating from Clamydomonas reinhardtii
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0001
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
0.0003
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
0.0005
0.0006
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
0.0013
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
0.0017
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
0.302
-
mutant enzyme C140S, at 30°C 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
5.75
10.3
-
wild type enzyme, at 30°C 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
additional information
0.0005
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
0.0005
Astragalus tephrosioides
-
enzyme reaction is initiated by the addition of crude protein extracts (0.015 mg of protein) and incubated at 30°C for 30 min
additional information
-
specificity runs though a maximum after 30 h of growth
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.5
7.6
9.5
9.5
-
reaction with cytochrome c as electron acceptor, Tris-HCl buffer
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 90
archaebacterium
-
70°C: about 65% of maximal activity, 90°C: about 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha subunit and beta subunit
B8PS61; B8DS74
UniProt
brenda
large subunit AprA and small subunit AprB
F6KEW4; F6KEW3
UniProt
brenda
O28603: adenylylsulfate reductase, O2860: subunit A adenylylsulfate reductase, subunit B
O28603; O28604
SwissProt
brenda
Q59339: alpha-subunit, Q59338: beta-subunit
SwissProt
brenda
aprA fragment; f.sp. thiosulfatophilum, strain DSM 245, gene aprA
UniProt
brenda
aprB fragment; f.sp. thiosulfatophilum, DSM 245, gene aprB
UniProt
brenda
G100A, ATCC27774, API, ATCC 13541, Norway; weak activity
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
APS reductase enhances strongly in the shoots of sulfate-deprived plants, and rapidly decreases again upon sulfate re-supply
brenda
additional information
-
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
brenda
additional information
-
extracts of sulfite-grown cells have lower activity than extracts of sulfate-grown cells
brenda
additional information
-
extracts of sulfite-grown cells have lower activity than extracts of sulfate-grown cells
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
mitochondrial or cytoplasmic localization
-
brenda
-
87% of the activity is located on the cytoplasmic side of the cytoplasmic membrane
-
brenda
Desulfovibrio vulgaris Marburg / DSM 2119
-
87% of the activity is located on the cytoplasmic side of the cytoplasmic membrane
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
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
physiological function
-
key enzyme of the dissimilatory sulfate respiration
physiological function
formation of a physical complex between adenosyl phosphosulfate reductase Apr and quinone-interacting membrane-bound oxidoreductase Qmo
physiological function
Q72DT2
formation of a physical complex between adenosyl phosphosulfate reductase Apr and quinone-interacting membrane-bound oxidoreductase Qmo
physiological function
-
coexpression of Escherichia coli aspartate kinase AKIII and Pseudomonas aeruginosa adenylylsulfate reductase in Medicago sativa. Compared to the wild-type alfalfa, the content of cysteine increases by 30% and that of methionine increases by 60%. A substantial increase in the abundance of essential amino acids, such as aspartate and lysine, is found. The total amino acid content and the forage biomass tested show no significant changes in the transgenic plants
physiological function
-
formation of a physical complex between adenosyl phosphosulfate reductase Apr and quinone-interacting membrane-bound oxidoreductase Qmo
-
physiological function
-
formation of a physical complex between adenosyl phosphosulfate reductase Apr and quinone-interacting membrane-bound oxidoreductase Qmo
-
physiological function
-
coexpression of Escherichia coli aspartate kinase AKIII and Pseudomonas aeruginosa adenylylsulfate reductase in Medicago sativa. Compared to the wild-type alfalfa, the content of cysteine increases by 30% and that of methionine increases by 60%. A substantial increase in the abundance of essential amino acids, such as aspartate and lysine, is found. The total amino acid content and the forage biomass tested show no significant changes in the transgenic plants
-
Show AA Sequence and Transmembrane Helices (915 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28603
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28603
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28603
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28603
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28603
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28603
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
-
1 * 18000 + 1 * 75000, containing one FAD per molecule and eight iron atoms arranged in two [4Fe-4S] clusters, SDS-PAGE
18500
2 * 80000 + 1 * 18500, alpha2beta structure, SDS-PAGE
20000
25600
-
alpha2beta2, 2 * 67800 + 2 * 25600, smallest catalytic active unit, SDS-PAGE
26000
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
28700
28710
30470
-
MALDI-TOF mass spectrometry, the enzyme used is a recombinant protein with 48 additional residues containing the His6 tag
67800
-
alpha2beta2, 2 * 67800 + 2 * 25600, smallest catalytic active unit, SDS-PAGE
70000
75000
80000
96000
-
non-reducing SDS-PAGE, 16% of the protein was present as a homodimer
160000
170000
175000
180000
186000
-
smallest catalytic active subunit, also aggregations of 324000 Da and 569000 Da are detected, gel filtration
600000
-
gel filtration, the majority of the protein is aggregated
20000
-
calculated from sequence of cDNA, C-terminal domain of EiAPR; MALDI-TOF mass spectrometry, C-terminal domain of EiAPR
20000
F6KEW4; 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)
28710
-
ESI-FTICR mass spectrometry; theoretical value based on the chemical formula
70000
F6KEW4; 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)
75000
-
1 * 18000 + 1 * 75000, containing one FAD per molecule and eight iron atoms arranged in two [4Fe-4S] clusters, SDS-PAGE
80000
2 * 80000 + 1 * 18500, alpha2beta structure, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
hexamer
-
APSR comprises six alphabeta-heterodimers that form a hexameric structure, X-ray crystallography
homodimer
monomer
oligomer
2 * 80000 + 1 * 18500, alpha2beta structure, SDS-PAGE
tetramer
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