DB code: S00314

CATH domain 3.40.50.620 : Rossmann fold Catalytic domain
E.C. 1.8.4.8
CSA
M-CSA
MACiE M0279

CATH domain Related DB codes (homologues)
3.40.50.620 : Rossmann fold S00549 S00316 S00317 S00318 S00315 T00085 T00249 D00300 M00177 M00178 T00106 T00114

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P17854 Phosphoadenosine phosphosulfate reductase
EC 1.8.4.8
PAPS reductase, thioredoxin dependent
PAdoPS reductase
3''-phosphoadenylylsulfate reductase
PAPS sulfotransferase
NP_417242.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490971.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01507 (PAPS_reduct)
[Graphical View]

KEGG enzyme name
phosphoadenylyl-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)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P17854 CYSH_ECOLI Adenosine 3'',5''-bisphosphate + sulfite + thioredoxin disulfide = 3''-phosphoadenylyl sulfate + thioredoxin. Homodimer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00920 Sulfur metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00054 C00094 C00343 C00080 C00053 C00342
E.C.
Compound Adenosine 3',5'-bisphosphate Sulfite Thioredoxin disulfide H+ 3'-phosphoadenylyl sulfate Reduced thioredoxin
Type amine group,nucleotide sulfite amide group,carbohydrate,disulfide bond,peptide/protein others amine group,nucleotide ,sulfate group amide group,carbohydrate,peptide/protein,sulfhydryl group
ChEBI 17985
48854
15378
17980
PubChem 159296
22132154
1100
1038
10214
1surA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1surA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]

References
[1]
Resource
Comments
Medline ID
PubMed ID 7731953
Journal Proteins
Year 1994
Volume 20
Pages 347-55
Authors Bork P, Koonin EV
Title A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity.
Related PDB
Related UniProtKB
[2]
Resource
Comments CHARACTERIZATION, AND MUTAGENESIS.
Medline ID 96061968
PubMed ID 7588765
Journal Eur J Biochem
Year 1995
Volume 233
Pages 347-56
Authors Berendt U, Haverkamp T, Prior A, Schwenn JD
Title Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis.
Related PDB
Related UniProtKB P17854
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID 97411695
PubMed ID 9261082
Journal Structure
Year 1997
Volume 5
Pages 895-906
Authors Savage H, Montoya G, Svensson C, Schwenn JD, Sinning I
Title Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
Related PDB 1sur
Related UniProtKB P17854
[4]
Resource
Comments
Medline ID
PubMed ID 9653199
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 8404-9
Authors Bick JA, Aslund F, Chen Y, Leustek T
Title Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11940598
Journal J Biol Chem
Year 2002
Volume 277
Pages 21786-91
Authors Kopriva S, Buchert T, Fritz G, Suter M, Benda R, Schunemann V, Koprivova A, Schurmann P, Trautwein AX, Kroneck PM, Brunold C
Title The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 12072441
Journal J Biol Chem
Year 2002
Volume 277
Pages 32606-15
Authors Williams SJ, Senaratne RH, Mougous JD, Riley LW, Bertozzi CR
Title 5'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteria.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-07-14 2009-02-26