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
ec00920  Sulfur metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K05907  adenylyl-sulfate reductase (glutathione)
Genes
RSS: 109440769 109441021
ATH: AT1G62180(APR2) AT4G04610(APR1) AT4G21990(APR3)
ALY: ARALYDRAFT_475126 ARALYDRAFT_911717 ARALYDRAFT_914435
CRB: 17880982 17883322 17896630
CSAT: 104703816 104707608 104714551 104716805 104718119 104722840 104731320 104737308 104752870
EUS: EUTSA_v10023459mg EUTSA_v10025134mg EUTSA_v10028642mg
BRP: 103839826 103848153 103859677 103861274
BNA: 106346634 106347879 106366895 106396567 106418321 106418329 106420885 106435512 106440433 106442702 111212167
BOE: 106306507 106310441 106319498 106342464
THJ: 104806307 104809496 104818752
TCC: 18597168
EGR: 104441413
CAM: 101505158
LJA: Lj4g3v0149340.1(Lj4g3v0149340.1) Lj6g3v1872560.1(Lj6g3v1872560.1)
FVE: 101296464
RCU: 8284186
JCU: 105649322
BVG: 104900978
SOE: 110792539
OSA: 4343348
DOSA: Os07t0509800-01(Os07g0509800)
OBR: 102709478
BDI: 100828269
ATS: 109738044(LOC109738044)
SBI: 8080734
ZMA: 103647705(aprl2) 606419(aprl1)
SITA: 101776145
MUS: 103975596
DCT: 110111790
ATR: 18445736
PPP: 112281535
CRE: CHLREDRAFT_131444(MET16)
OLU: OSTLU_13445(APR1)
APRO: F751_6755
 » 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 93:13377-82 (1996)
DOI:10.1073/pnas.93.23.13377
  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 93:13383-8 (1996)
DOI:10.1073/pnas.93.23.13383
  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 95:8404-9 (1998)
DOI:10.1073/pnas.95.14.8404
  Sequence
[ath:AT4G04610]
Other DBs
ExplorEnz - The Enzyme Database: 1.8.4.9
IUBMB Enzyme Nomenclature: 1.8.4.9
ExPASy - ENZYME nomenclature database: 1.8.4.9
BRENDA, the Enzyme Database: 1.8.4.9
CAS: 355840-27-6

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