EzCatDB: S00314

DB codeS00314
CATH domainDomain 13.40.50.620Catalytic domain
E.C.1.8.4.8
MACiEM0279

CATH domainRelated DB codes (homologues)
3.40.50.620S00549,S00316,S00317,S00318,S00315,T00085,T00249,D00300,M00177,M00178,T00106,T00114

Enzyme Name
Swiss-protKEGG

P17854
Protein namePhosphoadenosine phosphosulfate reductasephosphoadenylyl-sulfate reductase (thioredoxin)
PAPS reductase, thioredoxin-dependent
PAPS reductase
thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase
3'-phosphoadenylylsulfate reductase
thioredoxin:3'-phospho-adenylylsulfate reductase
phosphoadenosine-phosphosulfate reductase
adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxinoxidoreductase (3'-phosphoadenosine-5'-phosphosulfate-forming)
SynonymsEC 1.8.4.8
PAPS reductase, thioredoxin dependent
PAdoPS reductase
3''-phosphoadenylylsulfate reductase
PAPS sulfotransferase

KEGG pathways
MAP codePathways
MAP00920Sulfur metabolism

Swiss-prot:Accession NumberP17854
Entry nameCYSH_ECOLI
ActivityAdenosine 3'',5''-bisphosphate + sulfite + thioredoxin disulfide = 3''-phosphoadenylyl sulfate + thioredoxin.
SubunitHomodimer.
Subcellular locationCytoplasm.
Cofactor


SubstratesProducts
KEGG-idC00054C00094C00343C00080C00053C00342
CompoundAdenosine 3',5'-bisphosphateSulfiteThioredoxin disulfideH+3'-phosphoadenylyl sulfateReduced thioredoxin
Typeamine group,nucleotidesulfiteamide group,carbohydrate,disulfide bond,peptide/proteinothersamine group,nucleotide,sulfate groupamide group,carbohydrate,peptide/protein,sulfhydryl group
1surAUnboundUnboundUnbound
UnboundUnbound

Active-site residues
pdb
1surA

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]


references
[1]
PubMed ID7731953
JournalProteins
Year1994
Volume20
Pages347-55
AuthorsBork P, Koonin EV
TitleA P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.
[2]
CommentsCHARACTERIZATION, AND MUTAGENESIS.
Medline ID96061968
PubMed ID7588765
JournalEur J Biochem
Year1995
Volume233
Pages347-56
AuthorsBerendt U, Haverkamp T, Prior A, Schwenn JD
TitleReaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis.
Related Swiss-protP17854
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID97411695
PubMed ID9261082
JournalStructure
Year1997
Volume5
Pages895-906
AuthorsSavage H, Montoya G, Svensson C, Schwenn JD, Sinning I
TitleCrystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
Related PDB1sur
Related Swiss-protP17854
[4]
PubMed ID9653199
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages8404-9
AuthorsBick JA, Aslund F, Chen Y, Leustek T
TitleGlutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase.
[5]
PubMed ID11940598
JournalJ Biol Chem
Year2002
Volume277
Pages21786-91
AuthorsKopriva S, Buchert T, Fritz G, Suter M, Benda R, Schunemann V, Koprivova A, Schurmann P, Trautwein AX, Kroneck PM, Brunold C
TitleThe presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation.
[6]
PubMed ID12072441
JournalJ Biol Chem
Year2002
Volume277
Pages32606-15
AuthorsWilliams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR
Title5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria.


createdupdated
2004-07-142009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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