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
3''-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAPS sulfotransferase
PAdoPS reductase
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
1100
22132154
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