3-mercaptopyruvate sulfurtransferase
Details
- Name
- 3-mercaptopyruvate sulfurtransferase
- Kind
- protein
- Synonyms
- 2.8.1.2
- MST
- Rhodanese-like protein
- Gene Name
- sseA
- UniProtKB Entry
- P31142Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0005531|3-mercaptopyruvate sulfurtransferase MSTTWFVGADWLAEHIDDPEIQIIDARMASPGQEDRNVAQEYLNGHIPGAVFFDIEALSD HTSPLPHMLPRPETFAVAMRELGVNQDKHLIVYDEGNLFSAPRAWWMLRTFGVEKVSILG GGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVKVTDVLLASHENTAQIIDARPAARF NAEVDEPRPGLRRGHIPGALNVPWTELVREGELKTTDELDAIFFGRGVSYDKPIIVSCGS GVTAAVVLLALATLDVPNVKLYDGAWSEWGARADLPVEPVK
- Number of residues
- 281
- Molecular Weight
- 30811.55
- Theoretical pI
- 4.3
- GO Classification
- Functions3-mercaptopyruvate sulfurtransferase activity / thiosulfate sulfurtransferase activityProcessesresponse to antibioticComponentscytosol
- General Function
- Catalyzes the transfer of sulfur from 3-mercaptopyruvate to a thiol-containing acceptor to form an intramolecular disulfide releasing hydrogen sulfide and pyruvate (Probable). May be involved in the enhancement of bacterial growth inhibition by serine (PubMed:7982894).
- Specific Function
- 3-mercaptopyruvate sulfurtransferase activity
- Pfam Domain Function
- Rhodanese (PF00581)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0020627|3-mercaptopyruvate sulfurtransferase (sseA) ATGTCCACGACATGGTTTGTAGGAGCCGACTGGCTCGCCGAACATATTGATGACCCGGAA ATTCAGATTATCGATGCCCGCATGGCGTCGCCTGGACAGGAGGATCGTAACGTTGCTCAG GAGTATCTGAATGGACATATTCCCGGCGCAGTGTTTTTTGATATCGAAGCGCTTTCTGAT CACACTTCCCCGCTTCCGCACATGCTGCCGCGCCCGGAAACGTTCGCCGTGGCGATGCGT GAATTAGGCGTTAACCAGGATAAGCACCTGATTGTCTATGACGAAGGTAATCTTTTCTCA GCCCCACGAGCATGGTGGATGCTGCGCACCTTTGGTGTAGAGAAAGTGTCGATTCTGGGG GGTGGACTTGCAGGCTGGCAGCGCGATGATCTGCTGTTAGAAGAAGGTGCAGTAGAGCTG CCGGAAGGAGAGTTTAACGCCGCGTTTAATCCTGAAGCCGTGGTGAAAGTAACCGATGTA TTATTGGCAAGCCATGAAAATACGGCGCAAATTATTGATGCCCGCCCGGCTGCACGTTTT AACGCAGAAGTTGATGAACCTCGCCCAGGTTTACGTCGCGGACATATTCCCGGAGCACTG AATGTTCCGTGGACGGAACTGGTGCGCGAAGGCGAACTAAAAACGACCGATGAACTGGAT GCGATATTTTTTGGTCGCGGCGTCAGCTACGACAAACCAATTATCGTCAGCTGCGGCTCT GGTGTAACGGCAGCCGTGGTTTTGTTAGCACTCGCGACGCTGGATGTGCCAAACGTGAAA CTGTACGACGGCGCATGGAGTGAATGGGGCGCGCGGGCAGATTTACCGGTTGAGCCAGTG AAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P31142 UniProtKB Entry Name THTM_ECOLI GenBank Gene ID AP009048 PDB ID(s) 1URH KEGG ID ecj:JW2505 NCBI Gene ID 946993 - General References
- Hama H, Kayahara T, Ogawa W, Tsuda M, Tsuchiya T: Enhancement of serine-sensitivity by a gene encoding rhodanese-like protein in Escherichia coli. J Biochem. 1994 Jun;115(6):1135-40. [Article]
- Yamamoto Y, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kimura S, Kitagawa M, Makino K, Miki T, Mitsuhashi N, Mizobuchi K, Mori H, Nakade S, Nakamura Y, Nashimoto H, Oshima T, Oyama S, Saito N, Sampei G, Satoh Y, Sivasundaram S, Tagami H, Horiuchi T, et al.: Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features. DNA Res. 1997 Apr 28;4(2):91-113. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Colnaghi R, Cassinelli G, Drummond M, Forlani F, Pagani S: Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition. FEBS Lett. 2001 Jul 6;500(3):153-6. [Article]
- Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, Bordo D: The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli. J Mol Biol. 2004 Jan 9;335(2):583-93. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details S-Mercaptocysteine experimental unknown target Details