ID   THT2_CAEEL              Reviewed;         328 AA.
AC   O17730;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Putative thiosulfate sulfurtransferase mpst-1;
DE            EC=2.8.1.1;
DE   AltName: Full=Mercaptopyruvate sulfurtransferase homolog 1;
GN   Name=mpst-1; ORFNames=D2023.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=22131987; DOI=10.1155/2011/394970;
RA   Mathew N.D., Schlipalius D.I., Ebert P.R.;
RT   "Sulfurous gases as biological messengers and toxins: comparative genetics
RT   of their metabolism in model organisms.";
RL   J. Toxicol. 2011:394970-394984(2011).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=24093496; DOI=10.1089/ars.2013.5448;
RA   Qabazard B., Li L., Gruber J., Peh M.T., Ng L.F., Kumar S.D., Rose P.,
RA   Tan C.H., Dymock B.W., Wei F., Swain S.C., Halliwell B., Sturzenbaum S.R.,
RA   Moore P.K.;
RT   "Hydrogen sulfide is an endogenous regulator of aging in Caenorhabditis
RT   elegans.";
RL   Antioxid. Redox Signal. 20:2621-2630(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC         thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC         ChEBI:CHEBI:33542; EC=2.8.1.1;
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   -!- DISRUPTION PHENOTYPE: Knockdown and RNAi cause reduced lifespan.
CC       Knockdown reduced brood size and halved the production of H(2)S.
CC       {ECO:0000269|PubMed:24093496}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z81052; CAB02870.1; -; Genomic_DNA.
DR   PIR; T20344; T20344.
DR   RefSeq; NP_505979.1; NM_073578.4.
DR   AlphaFoldDB; O17730; -.
DR   SMR; O17730; -.
DR   BioGRID; 44642; 3.
DR   STRING; 6239.D2023.5; -.
DR   EPD; O17730; -.
DR   PaxDb; O17730; -.
DR   PeptideAtlas; O17730; -.
DR   EnsemblMetazoa; D2023.5.1; D2023.5.1; WBGene00008409.
DR   GeneID; 179617; -.
DR   KEGG; cel:CELE_D2023.5; -.
DR   UCSC; D2023.5; c. elegans.
DR   CTD; 179617; -.
DR   WormBase; D2023.5; CE09075; WBGene00008409; mpst-1.
DR   eggNOG; KOG1529; Eukaryota.
DR   GeneTree; ENSGT00510000046773; -.
DR   HOGENOM; CLU_847929_0_0_1; -.
DR   InParanoid; O17730; -.
DR   OMA; RNLPHMM; -.
DR   OrthoDB; 1553525at2759; -.
DR   PhylomeDB; O17730; -.
DR   PRO; PR:O17730; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00008409; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; 1.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   3: Inferred from homology;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..328
FT                   /note="Putative thiosulfate sulfurtransferase mpst-1"
FT                   /id="PRO_0000139404"
FT   DOMAIN          22..162
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          202..320
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        278
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ   SEQUENCE   328 AA;  36948 MW;  35190DD7928DA213 CRC64;
     MSLKKIIDVK SVNTLLKKGI INKEGVRIID CSFAVAPRPD WKEFEQEGYG DFKNLMAEPS
     PSRNLYLAGH IPEAVHVDLD IATYPSRYQR FQQYRADLFE EYAQMVGLNN KEHFIFYGKG
     AFGGMLFASK VAWIFKSYGH ENISLVDGGF DSWKRNGFEV STELVKLPAG NFKAEDNFKK
     YVITFQELEA KKDGEDKQFI EKTSEINFLD SRIRGQFDGT QETGLDPHLV NGTRIAGFKN
     LPSAELLVKG GNLKSEEEIK SWLTQNGYVE NQPTITSCNA GIQAALLAYV IDAVKPSQNP
     PRVYNGSLKE MELRAPKKIS EGPQHLPH