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 17985 |
48854 48854 |
15378 15378 |
17980 17980 |
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| PubChem |
159296 159296 |
1100 22132154 1100 22132154 |
1038 1038 |
10214 10214 |
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| 1surA |
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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 |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
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[3]
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| 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, |
| 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 |
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| Created | Updated |
|---|---|
| 2004-07-14 | 2009-02-26 |