THTM_SCHPO
ID THTM_SCHPO Reviewed; 298 AA.
AC Q9USJ1; Q9URT3;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable 3-mercaptopyruvate sulfurtransferase;
DE Short=MST;
DE EC=2.8.1.2;
GN Name=tum1; ORFNames=SPCC4B3.01, SPCP25A2.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Required for formation of the 2-thio group of the 5-
CC methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
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; CU329672; CAB60675.1; -; Genomic_DNA.
DR PIR; T50448; T50448.
DR RefSeq; XP_001713164.1; XM_001713112.2.
DR AlphaFoldDB; Q9USJ1; -.
DR SMR; Q9USJ1; -.
DR BioGRID; 857852; 1.
DR STRING; 4896.SPCC4B3.01.1; -.
DR iPTMnet; Q9USJ1; -.
DR MaxQB; Q9USJ1; -.
DR PaxDb; Q9USJ1; -.
DR PRIDE; Q9USJ1; -.
DR EnsemblFungi; SPCC4B3.01.1; SPCC4B3.01.1:pep; SPCC4B3.01.
DR PomBase; SPCC4B3.01; tum1.
DR VEuPathDB; FungiDB:SPCC4B3.01; -.
DR eggNOG; KOG1529; Eukaryota.
DR HOGENOM; CLU_031618_3_0_1; -.
DR InParanoid; Q9USJ1; -.
DR OMA; LLDVRWQ; -.
DR PhylomeDB; Q9USJ1; -.
DR Reactome; R-SPO-1614558; Degradation of cysteine and homocysteine.
DR PRO; PR:Q9USJ1; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; ISO:PomBase.
DR GO; GO:1990799; P:mitochondrial tRNA wobble position uridine thiolation; ISO:PomBase.
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 1: Evidence at protein level;
KW Mitochondrion; Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..298
FT /note="Probable 3-mercaptopyruvate sulfurtransferase"
FT /id="PRO_0000139401"
FT DOMAIN 24..141
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 176..292
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 142..175
FT /note="Hinge"
FT ACT_SITE 252
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 298 AA; 32800 MW; DC3D7F6AAA770623 CRC64;
MFSVGKKISF ILPIKGVLQK LKDNAQKTVL LDATWYLPTD TKNGKKEYLE SRLPGAQYFD
IDEAKDHKNP LPHMLPPADE FASYVGKLGI DRNTNVIIYD RKGFFSSPRV FWTFKVFGHE
HVFLFPNAFN AWKTEGLELE TGEPRTPKPV VYEGAKLNKD LVASFDDIVK VIESPDAAGV
HIVDARAHER FLGNVPESRP GLASGHIPTS INIPFTETTA AGITAPKPEE DLEKVFSSHG
LTDKSVPIIT SCGSGVTASV LFAALKECGF KDVRVYDESW SGYGKRANED SSLLATGP
