THTM_ECO57
ID THTM_ECO57 Reviewed; 281 AA.
AC P58388;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=3-mercaptopyruvate sulfurtransferase {ECO:0000250|UniProtKB:P31142};
DE Short=MST {ECO:0000250|UniProtKB:P31142};
DE EC=2.8.1.2 {ECO:0000250|UniProtKB:P31142};
DE AltName: Full=Rhodanese-like protein {ECO:0000250|UniProtKB:P31142};
GN Name=sseA; OrderedLocusNames=Z3788, ECs3387;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Catalyzes the transfer of sulfur from 3-mercaptopyruvate to a
CC thiol-containing acceptor to form an intramolecular disulfide releasing
CC hydrogen sulfide and pyruvate. {ECO:0000250|UniProtKB:P31142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol =
CC [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate;
CC Xref=Rhea:RHEA:21740, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57678; EC=2.8.1.2;
CC Evidence={ECO:0000250|UniProtKB:P31142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21741;
CC Evidence={ECO:0000250|UniProtKB:P31142};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal region is the non-catalytic domain; the C-
CC terminus contains the active-site cysteine residue and the CGSGVTA
CC motif probably responsible for substrate specificity.
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57635.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB36810.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57635.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36810.1; ALT_INIT; Genomic_DNA.
DR PIR; C91052; C91052.
DR PIR; G85896; G85896.
DR RefSeq; NP_311414.2; NC_002695.1.
DR RefSeq; WP_000108625.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58388; -.
DR SMR; P58388; -.
DR STRING; 155864.EDL933_3682; -.
DR EnsemblBacteria; AAG57635; AAG57635; Z3788.
DR EnsemblBacteria; BAB36810; BAB36810; ECs_3387.
DR GeneID; 915202; -.
DR KEGG; ece:Z3788; -.
DR KEGG; ecs:ECs_3387; -.
DR PATRIC; fig|386585.9.peg.3538; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_3_0_6; -.
DR OMA; QRPGHVP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364; PTHR11364; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..281
FT /note="3-mercaptopyruvate sulfurtransferase"
FT /id="PRO_0000139410"
FT DOMAIN 17..135
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 165..278
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 238..244
FT /note="Substrate specificity"
FT /evidence="ECO:0000255"
FT ACT_SITE 238
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 30826 MW; 6751492A3AB30016 CRC64;
MSTTWFVGAD WLAEHIDDPE IQIIDARMAS PGQEDRNVAQ EYLNGHIPGA VFFDIEALSD
HTSPLPHMLP RPETFAVAMR ELGVNQDKHL IVYDEGNLFS APRAWWMLRT FGVEKVSILG
GGLAGWQRDD LLLEEGAVEL PEGEFNAAFN PEAVVKVTDV LLASHENTAQ IIDARPAARF
NAEVDEPRPG LRRGHIPGAL NVPWTELVRE GELKTTDELD AIFFGRGVSY DKPIIVSCGS
GVTAAVVLLA LATLDVPNVK LYDGAWSEWG ARADLPVEPL K
