THTM_ECOLI
ID THTM_ECOLI Reviewed; 281 AA.
AC P31142; P78096;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=3-mercaptopyruvate sulfurtransferase;
DE Short=MST;
DE EC=2.8.1.2 {ECO:0000305|PubMed:11445076};
DE AltName: Full=Rhodanese-like protein;
GN Name=sseA; OrderedLocusNames=b2521, JW2505;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / W3133-2;
RX PubMed=7982894; DOI=10.1093/oxfordjournals.jbchem.a124469;
RA Hama H., Kayahara T., Ogawa W., Tsuda M., Tsuchiya T.;
RT "Enhancement of serine-sensitivity by a gene encoding rhodanese-like
RT protein in Escherichia coli.";
RL J. Biochem. 115:1135-1140(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-240.
RX PubMed=11445076; DOI=10.1016/s0014-5793(01)02610-2;
RA Colnaghi R., Cassinelli G., Drummond M., Forlani F., Pagani S.;
RT "Properties of the Escherichia coli rhodanese-like protein SseA:
RT contribution of the active-site residue Ser240 to sulfur donor
RT recognition.";
RL FEBS Lett. 500:153-156(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=14672665; DOI=10.1016/j.jmb.2003.10.072;
RA Spallarossa A., Forlani F., Carpen A., Armirotti A., Pagani S.,
RA Bolognesi M., Bordo D.;
RT "The 'rhodanese' fold and catalytic mechanism of 3-mercaptopyruvate
RT sulfurtransferases: crystal structure of SseA from Escherichia coli.";
RL J. Mol. Biol. 335:583-593(2004).
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 (Probable). May be involved in the
CC enhancement of bacterial growth inhibition by serine (PubMed:7982894).
CC {ECO:0000269|PubMed:7982894, ECO:0000305|PubMed:11445076}.
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:0000305|PubMed:11445076};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21741;
CC Evidence={ECO:0000305|PubMed:11445076};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14672665}.
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=BAA01382.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D10496; BAA01382.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC75574.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16411.2; -; Genomic_DNA.
DR PIR; H65028; H65028.
DR RefSeq; NP_417016.4; NC_000913.3.
DR RefSeq; WP_000108626.1; NZ_STEB01000011.1.
DR PDB; 1URH; X-ray; 2.80 A; A/B=2-281.
DR PDBsum; 1URH; -.
DR AlphaFoldDB; P31142; -.
DR SMR; P31142; -.
DR BioGRID; 4260592; 28.
DR DIP; DIP-10921N; -.
DR IntAct; P31142; 1.
DR STRING; 511145.b2521; -.
DR DrugBank; DB02761; S-Mercaptocysteine.
DR jPOST; P31142; -.
DR PaxDb; P31142; -.
DR PRIDE; P31142; -.
DR EnsemblBacteria; AAC75574; AAC75574; b2521.
DR EnsemblBacteria; BAA16411; BAA16411; BAA16411.
DR GeneID; 66673591; -.
DR GeneID; 946993; -.
DR KEGG; ecj:JW2505; -.
DR KEGG; eco:b2521; -.
DR PATRIC; fig|1411691.4.peg.4215; -.
DR EchoBASE; EB1557; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_3_0_6; -.
DR InParanoid; P31142; -.
DR OMA; QRPGHVP; -.
DR PhylomeDB; P31142; -.
DR BioCyc; EcoCyc:EG11600-MON; -.
DR BioCyc; MetaCyc:EG11600-MON; -.
DR BRENDA; 2.8.1.2; 2026.
DR EvolutionaryTrace; P31142; -.
DR PRO; PR:P31142; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IDA:EcoCyc.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:EcoCyc.
DR GO; GO:0042262; P:DNA protection; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..281
FT /note="3-mercaptopyruvate sulfurtransferase"
FT /id="PRO_0000139409"
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 BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 240
FT /note="S->A: Decrease in 3-mercaptopyruvate cyanide
FT sulfurtransferase activity; abolition of thiosulfate
FT binding."
FT /evidence="ECO:0000269|PubMed:11445076"
FT MUTAGEN 240
FT /note="S->K: Decrease in 3-mercaptopyruvate cyanide
FT sulfurtransferase activity; increased affinity for
FT thiosulfate."
FT /evidence="ECO:0000269|PubMed:11445076"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:1URH"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:1URH"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1URH"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1URH"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1URH"
SQ SEQUENCE 281 AA; 30812 MW; 6744A92A3AB30016 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 ARADLPVEPV K
