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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: Q313I5
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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, adenylyl-sulfate reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AprA
Oleidesulfovibrio alaskensis
alpha-subunit
Dde_1110
Oleidesulfovibrio alaskensis
-
adenosine 5'-phosphosulfate reductase
-
-
-
-
adenosine phosphosulfate reductase
-
-
-
-
AdoPSO4 reductase
-
-
-
-
AMP,sulfite:flavin oxidoreductase
-
-
-
-
APS reductase
-
-
-
-
APS-reductase
-
-
-
-
reductase, adenylylsulfate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Oleidesulfovibrio alaskensis
alpha-subunit AprA
UniProt
Manually annotated by BRENDA team
Oleidesulfovibrio alaskensis G20
alpha-subunit AprA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Oleidesulfovibrio alaskensis
formation of a physical complex between adenosyl phosphosulfate reductase Apr and quinone-interacting membrane-bound oxidoreductase Qmo
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q313I5_OLEA2
Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
664
0
74655
TrEMBL
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Krumholz, L.R.; Wang, L.; Beck, D.A.; Wang, T.; Hackett, M.; Mooney, B.; Juba, T.R.; McInerney, M.J.; Meyer, B.; Wall, J.D.; Stahl, D.A.
Membrane protein complex of APS reductase and Qmo is present in Desulfovibrio vulgaris and Desulfovibrio alaskensis
Microbiology
159
2162-2168
2013
Oleidesulfovibrio alaskensis (Q313I5), Desulfovibrio vulgaris (Q72DT2), Desulfovibrio vulgaris, Oleidesulfovibrio alaskensis G20 (Q313I5), Desulfovibrio vulgaris Hildenborough (Q72DT2)
Manually annotated by BRENDA team