THTM_PSEAE
ID THTM_PSEAE Reviewed; 284 AA.
AC Q9I452;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable 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;
GN Name=sseA; OrderedLocusNames=PA1292;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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}.
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DR EMBL; AE004091; AAG04681.1; -; Genomic_DNA.
DR PIR; D83485; D83485.
DR RefSeq; NP_249983.1; NC_002516.2.
DR RefSeq; WP_003109274.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I452; -.
DR SMR; Q9I452; -.
DR STRING; 287.DR97_643; -.
DR PaxDb; Q9I452; -.
DR PRIDE; Q9I452; -.
DR DNASU; 881495; -.
DR EnsemblBacteria; AAG04681; AAG04681; PA1292.
DR GeneID; 881495; -.
DR KEGG; pae:PA1292; -.
DR PATRIC; fig|208964.12.peg.1342; -.
DR PseudoCAP; PA1292; -.
DR HOGENOM; CLU_031618_0_0_6; -.
DR InParanoid; Q9I452; -.
DR OMA; LLDVRWQ; -.
DR PhylomeDB; Q9I452; -.
DR BioCyc; PAER208964:G1FZ6-1317-MON; -.
DR Proteomes; UP000002438; 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; IBA:GO_Central.
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; 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; PS50206; RHODANESE_3; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Repeat; Transferase.
FT CHAIN 1..284
FT /note="Probable 3-mercaptopyruvate sulfurtransferase"
FT /id="PRO_0000139411"
FT DOMAIN 17..138
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 168..281
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 241..247
FT /note="Substrate specificity"
FT /evidence="ECO:0000250"
FT ACT_SITE 241
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 284 AA; 30598 MW; 2041E6AA7CA5A6C3 CRC64;
MSSAQLLTAQ QLAARLSEPD LLVLDCRFAL EDPSYGARVY QENHIPGAHF ADLERDLSAP
VRKGVTGRHP LPDPAELALK LQAWGLRQDS QVVLYDDGPG AFAARAWWLL HWLGKRDGVY
LLDGGLAAWK AAGLALTNGE SSLRPGDFQG QPDASLLIDA ATLQAQLGQP GLALLDARAQ
PRFRGEVEPI DPVAGHIPGA QCAAFTDNLG SDGRFLPPEQ LHQRFSALLR GRPVDELVAY
CGSGVTACHN LFALSLAGFP LPRLYAGSWS EWITDPRRPV ATGD
