KEGG   ENZYME: 1.8.4.9Help
Entry
EC 1.8.4.9                  Enzyme                                 

Name
adenylyl-sulfate reductase (glutathione);
5'-adenylylsulfate reductase (also used for EC 1.8.99.2);
AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming);
plant-type 5'-adenylylsulfate reductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With a disulfide as acceptor
BRITE hierarchy
Sysname
AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming)
Reaction(IUBMB)
AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione [RN:R05717]
Reaction(KEGG)
Substrate
AMP [CPD:C00020];
sulfite [CPD:C00094];
glutathione disulfide [CPD:C00127]
Product
adenylyl sulfate [CPD:C00224];
glutathione [CPD:C00051]
Comment
This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase, in using glutathione as the reductant. Glutathione can be replaced by gamma-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.
History
EC 1.8.4.9 created 2000, modified 2002
Pathway
Sulfur metabolism
Microbial metabolism in diverse environments
Orthology
K05907  
adenylyl-sulfate reductase (glutathione)
Genes
ATH: 
AT1G62180(APR2) AT4G04610(APR1) AT4G21990(APR3)
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
TCC: 
GMX: 
PVU: 
CAM: 
FVE: 
PPER: 
CSV: 
RCU: 
POP: 
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os07t0509800-01(Os07g0509800)
OBR: 
BDI: 
SBI: 
SORBI_02g034370(SORBIDRAFT_02g034370)
ZMA: 
606419(aprl1) 606480(aprl2)
SITA: 
ATR: 
s00037p00207940(AMTR_s00037p00207940)
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
OTA: 
MIS: 
MPP: 
BPG: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
 » show all
Taxonomy
Reference
1  [PMID:8917599]
  Authors
Gutierrez-Marcos JF, Roberts MA, Campbell EI, Wray JL.
  Title
Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and "APS reductase" activity.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 13377-82.
  Organism
Arabidopsis thaliana
  Sequence
Reference
2  [PMID:8917600]
  Authors
Setya A, Murillo M, Leustek T.
  Title
Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 13383-8.
  Organism
Arabidopsis thaliana
  Sequence
[ath:AT4G04610]
Reference
3  [PMID:9653199]
  Authors
Bick JA, Aslund F, Chen Y, Leustek T.
  Title
Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 8404-9.
  Organism
Arabidopsis thaliana
  Sequence
[ath:AT4G04610]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
355840-27-6

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