| Identification |
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| Name: | Phosphoadenosine phosphosulfate reductase |
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| Synonyms: | - 3'-phosphoadenylylsulfate reductase
- PAPS reductase, thioredoxin dependent
- PAPS sulfotransferase
- PAdoPS reductase
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| Gene Name: | cysH |
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| Enzyme Class: | |
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| Biological Properties |
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| General Function: | Involved in phosphoadenylyl-sulfate reductase (thioredoxin) activity |
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| Specific Function: | Reduction of activated sulfate into sulfite |
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| Cellular Location: | Cytoplasm |
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| SMPDB Pathways: | - Sulfur metabolism PW000922
- cysteine biosynthesis PW000800
- sulfur metabolism (butanesulfonate) PW000923
- sulfur metabolism (ethanesulfonate) PW000925
- sulfur metabolism (isethionate) PW000926
- sulfur metabolism (methanesulfonate) PW000927
- sulfur metabolism (propanesulfonate) PW000924
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| KEGG Pathways: | |
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| KEGG Reactions: | |
1.0Thioredoxin | + | 1.0 | + | 1.0Thioredoxin disulfide | ↔ | 1.0Thioredoxin disulfide | + | 1.0 | + | 1.0 | + | 1.0 |
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| SMPDB Reactions: | |
1.0 | + | 1.0reduced thioredoxin | → | 1.0Sulfite | + | 2.0 | + | 1.0Adenosine 3',5'-diphosphate | + | 2.0oxidized thioredoxin | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0reduced thioredoxin | → | 1.0Sulfite | + | 1.0oxidized thioredoxin | + | 1.0 | + | 1.0Adenosine 3',5'-diphosphate | + | 1.0 | + | 1.0 |
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| Complex Reactions: | |
1.0glutaredoxin | + | 1.0 | → | 1.0glutaredoxin | + | 2.0 | + | 1.0 | + | 1.0 |
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1.0 | + | 1.0Reduced Thioredoxin | → | 2.0 | + | 1.0 | + | 1.0 | + | 1.0Oxidized Thioredoxin |
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1.0 | + | 1.0 | + | 1.0thioredoxin disulfide | → | 1.0 | + | 1.0thioredoxin |
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| Metabolites: | |
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| GO Classification: | | Function |
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| catalytic activity | | oxidoreductase activity | | oxidoreductase activity, acting on a sulfur group of donors | | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor | | phosphoadenylyl-sulfate reductase (thioredoxin) activity | | Process |
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| cellular amino acid and derivative metabolic process | | cellular amino acid metabolic process | | cellular metabolic process | | cysteine biosynthetic process | | metabolic process | | oxidation reduction | | sulfate assimilation | | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) | | sulfur amino acid biosynthetic process | | sulfur amino acid metabolic process | | sulfur metabolic process |
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| Gene Properties |
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| Blattner: | b2762 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 62.19 |
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| Left Sequence End | 2885600 |
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| Right Sequence End | 2886334 |
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| Gene Sequence: | >735 bp
ATGAAAATTGACCTGAACGCCGATCTGGGCGAAGGCTGCGCCAGCGACGCAGAGCTATTA
ACGCTGGTTTCCTCTGCCAATATTGCCTGTGGATTTCATGCAGGCGATGCGCAAATCATG
CAGGCTTGCGTGCGTGAAGCAATAAAAAATGGTGTCGCGATTGGCGCTCACCCGAGTTTT
CCCGACAGGGAAAATTTTGGTCGCAGCGCCATGCAGCTGCCGCCAGAAACCGTTTACGCC
CAGACGCTGTATCAAATTGGCGCGCTGGCAACGATTGCCCGTGCGCAAGGCGGCGTAATG
CGTCATGTCAAACCGCACGGCATGTTGTACAACCAGGCGGCGAAAGAAGCACAACTGGCA
GACGCCATCGCCAGAGCGGTATACGCTTGCGATCCAGCATTGATTCTCGTCGGGCTGGCG
GGAAGCGAGCTGATTCGTGCAGGCAAGCAATATGGTCTGACAACGCGCGAGGAAGTGTTT
GCCGATCGCGGTTATCAGGCTGACGGCTCGCTGGTGCCGCGAAGCCAGTCAGGCGCGTTG
ATTGAAAACGAAGAACAGGCGCTGGCGCAAACGCTGGAGATGGTGCAACACGGCAGAGTC
AAAAGTATCACCGGCGAATGGGCAACGGTCGCGGCGCAAACGGTCTGCCTGCATGGCGAC
GGCGAGCACGCACTGGCGTTCGCCCGCCGACTACGCTCTGCATTTGCCGAAAAGGGGATT
GTTGTCGCAGCATAA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 244 |
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| Protein Molecular Weight: | 27976 |
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| Protein Theoretical pI: | 5 |
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| PDB File: | 1SUR |
| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >Phosphoadenosine phosphosulfate reductase
MSKLDLNALNELPKVDRILALAETNAELEKLDAEGRVAWALDNLPGEYVLSSSFGIQAAV
SLHLVNQIRPDIPVILTDTGYLFPETYRFIDELTDKLKLNLKVYRATESAAWQEARYGKL
WEQGVEGIEKYNDINKVEPMNRALKELNAQTWFAGLRREQSGSRANLPVLAIQRGVFKVL
PIIDWDNRTIYQYLQKHGLKYHPLWDEGYLSVGDTHTTRKWEPGMAEEETRFFGLKRECG
LHEG |
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| References |
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| External Links: | |
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| General Reference: | - Berendt, U., Haverkamp, T., Prior, A., Schwenn, J. D. (1995). "Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis." Eur J Biochem 233:347-356. Pubmed: 7588765
- Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Krone, F. A., Westphal, G., Meyer, H. E., Schwenn, J. D. (1990). "PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H." FEBS Lett 260:6-9. Pubmed: 2404794
- Krone, F. A., Westphal, G., Schwenn, J. D. (1991). "Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli." Mol Gen Genet 225:314-319. Pubmed: 2005873
- Ostrowski, J., Wu, J. Y., Rueger, D. C., Miller, B. E., Siegel, L. M., Kredich, N. M. (1989). "Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase." J Biol Chem 264:15726-15737. Pubmed: 2670946
- Savage, H., Montoya, G., Svensson, C., Schwenn, J. D., Sinning, I. (1997). "Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases." Structure 5:895-906. Pubmed: 9261082
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