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THT1_CAEEL
ID   THT1_CAEEL              Reviewed;         277 AA.
AC   P91247;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Putative thiosulfate sulfurtransferase mpst-4;
DE            EC=2.8.1.1 {ECO:0000250|UniProtKB:P00586};
DE   AltName: Full=Mercaptopyruvate sulfurtransferase homolog 4 {ECO:0000312|WormBase:F11G11.9};
GN   Name=mpst-4 {ECO:0000312|WormBase:F11G11.9};
GN   ORFNames=F11G11.9 {ECO:0000312|WormBase:F11G11.9};
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   INDUCTION.
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         Evidence={ECO:0000250|UniProtKB:P00586};
CC   -!- INDUCTION: Expression increased by knockdown of mpst-1.
CC       {ECO:0000269|PubMed:24093496}.
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.
CC       {ECO:0000250|UniProtKB:P00586}.
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DR   EMBL; FO081119; CCD69260.1; -; Genomic_DNA.
DR   PIR; T29979; T29979.
DR   RefSeq; NP_001309500.1; NM_001322727.1.
DR   AlphaFoldDB; P91247; -.
DR   SMR; P91247; -.
DR   STRING; 6239.F11G11.9; -.
DR   PaxDb; P91247; -.
DR   PeptideAtlas; P91247; -.
DR   EnsemblMetazoa; F11G11.9.1; F11G11.9.1; WBGene00017387.
DR   GeneID; 173838; -.
DR   KEGG; cel:CELE_F11G11.9; -.
DR   UCSC; F11G11.9; c. elegans.
DR   CTD; 173838; -.
DR   WormBase; F11G11.9; CE51449; WBGene00017387; mpst-4.
DR   eggNOG; KOG1529; Eukaryota.
DR   GeneTree; ENSGT00510000046773; -.
DR   HOGENOM; CLU_076711_0_0_1; -.
DR   InParanoid; P91247; -.
DR   OMA; AIVIKIE; -.
DR   OrthoDB; 1553525at2759; -.
DR   PhylomeDB; P91247; -.
DR   PRO; PR:P91247; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00017387; Expressed in material anatomical entity and 2 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; 2.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   2: Evidence at transcript level;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..277
FT                   /note="Putative thiosulfate sulfurtransferase mpst-4"
FT                   /id="PRO_0000139403"
FT   DOMAIN          15..153
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          155..243
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        204
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ   SEQUENCE   277 AA;  30699 MW;  25EDF666CE12824C CRC64;
     MAVDMIVEPK WVVQNFGNIR ILDASWTFKP KADVAEYKAK YYNKFGVGMN ELKNPEYLAE
     HINGAAHFNF DIAYYPSEDE RFTLYTPEEF SSYVKRLGVF NGDHLVIYGR GKDGGMAAAS
     RAYWTFRYYG YTTVSVLNGG IEAFKLAQGV VQSDSKAEGI RCKDAIHFPI GEVCAAKGFK
     KKTDCDQAFA AKGIKVGDTV VISCGIGLSA SAICLAAARS GIVAKLYNGG VHELAYKAPQ
     HLNMRVTLLL HAITVLRCTY IHFTFLYAIV IKIERIV
 
 
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