KEGG   ENZYME: 1.8.4.10Help
Entry
EC 1.8.4.10                 Enzyme                                 

Name
adenylyl-sulfate reductase (thioredoxin);
thioredoxin-dependent 5'-adenylylsulfate reductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With a disulfide as acceptor
BRITE hierarchy
Sysname
AMP,sulfite:thioredoxin-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming)
Reaction(IUBMB)
AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin [RN:R07176]
Reaction(KEGG)
Substrate
AMP [CPD:C00020];
sulfite [CPD:C00094];
thioredoxin disulfide [CPD:C00343]
Product
5'-adenylyl sulfate [CPD:C00224];
thioredoxin [CPD:C00342]
Comment
Uses adenylyl sulfate, not phosphoadenylyl sulfate, distinguishing this enzyme from EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin). Uses thioredoxin as electron donor, not glutathione or other donors, distinguishing it from EC 1.8.4.9 [adenylyl-sulfate reductase (glutathione)] and EC 1.8.99.2 (adenylyl-sulfate reductase).
History
EC 1.8.4.10 created 2003
Reference
1  [PMID:10613872]
  Authors
Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T.
  Title
Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria.
  Journal
J. Bacteriol. 182 (2000) 135-42.
  Organism
Burkholderia cepacia
  Sequence
[up:Q9RFS6]
Reference
2  [PMID:10464198]
  Authors
Abola AP, Willits MG, Wang RC, Long SR.
  Title
Reduction of adenosine-5'-phosphosulfate instead of 3'-phosphoadenosine-5'-phosphosulfate in cysteine biosynthesis by Rhizobium meliloti and other members of the family Rhizobiaceae.
  Journal
J. Bacteriol. 181 (1999) 5280-7.
  Organism
Rhizobium meliloti
Reference
3  [PMID:12072441]
  Authors
Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR.
  Title
5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria.
  Journal
J. Biol. Chem. 277 (2002) 32606-15.
  Organism
Mycobacterium smegmatis [GN:msm], Mycobacterium tuberculosis [GN:mtc mra]
Reference
4  [PMID:10939523]
  Authors
Neumann S, Wynen A, Truper HG, Dahl C.
  Title
Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway.
  Journal
Mol. Biol. Rep. 27 (2000) 27-33.
  Organism
Allochromatium vinosum
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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