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
Functions
3-mercaptopyruvate sulfurtransferase activity / thiosulfate sulfurtransferase activity
Processes
response to antibiotic
Components
cytosol
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
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
ResourceLink
UniProtKB IDP31142
UniProtKB Entry NameTHTM_ECOLI
GenBank Gene IDAP009048
PDB ID(s)1URH
KEGG IDecj:JW2505
NCBI Gene ID946993
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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
DrugDrug groupPharmacological action?TypeActionsDetails
S-MercaptocysteineexperimentalunknowntargetDetails