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Information on EC 1.8.99.2 - adenylyl-sulfate reductase

for references in articles please use BRENDA:EC1.8.99.2
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EC Tree
IUBMB Comments
An iron flavoprotein (FAD). Methyl viologen can act as acceptor.
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This record set is specific for:
UNIPROT: O28603
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Word Map
  • 1.8.99.2
  • resection
  • abdominoperineal
  • rectal
  • postoperative
  • women
  • anal
  • perineal
  • pelvic
  • preoperative
  • acute-phase
  • 5-year
  • curative
  • laparoscopic
  • rust
  • demographic
  • radiotherapy
  • oncological
  • admission
  • c-reactive
  • population-based
  • neoadjuvant
  • anorectal
  • puccinia
  • sphincter
  • intraoperative
  • colostomy
  • tritici
  • verge
  • chemoradiation
  • chemoradiotherapy
  • ontario
  • circumferential
  • haptoglobin
  • flap
  • poisson
  • incontinence
  • abdominis
  • zoledronic
  • stoma
  • mesorectal
  • dehiscence
  • anastomosis
  • exenteration
  • synthesis
  • analysis
  • ileostomy
  • levator
  • agriculture
  • environmental protection
  • actuarial
  • log-binomial
  • orthoped
  • race-specific
  • psycinfo
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
apr, aprba, adenylylsulfate reductase, aps-reductase, adenosine phosphosulfate reductase, adenylyl sulfate reductase, acapr1, adopso4 reductase, adenylylsulphate reductase, dissimilatory aps reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine 5'-phosphosulfate reductase
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adenosine 5'-phosphosulfate reductase
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-
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adenosine phosphosulfate reductase
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-
-
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AdoPSO4 reductase
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-
-
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AMP,sulfite:flavin oxidoreductase
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-
-
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APS reductase
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-
-
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APS-reductase
-
-
-
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reductase, adenylylsulfate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming)
An iron flavoprotein (FAD). Methyl viologen can act as acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-75-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenylyl sulfate + reduced acceptor
AMP + sulfite + acceptor
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
flavoenzyme.The two electrons required for adenylyl sulfate reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4Fe-4S cluster
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O28603_ARCFU
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
643
0
73270
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fritz, G.; Roth, A.; Schiffer, A.; Buchert, T.; Bourenkov, G.; Bartunik, H.D.; Huber, H.; Stetter, K.O.; Kroneck, P.M.H.; Ermler, U.
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution
Proc. Natl. Acad. Sci. USA
99
1836-1841
2002
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O28603)
Manually annotated by BRENDA team