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HMT2_SCHPO
ID   HMT2_SCHPO              Reviewed;         459 AA.
AC   O94284; O13293;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial;
DE            EC=1.8.5.- {ECO:0000269|PubMed:10224084};
DE   AltName: Full=Cadmium resistance protein 1;
DE   AltName: Full=Heavy metal tolerance protein 2;
DE   Flags: Precursor;
GN   Name=hmt2; Synonyms=cad1; ORFNames=SPBC2G5.06c;
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 [GENOMIC DNA], FUNCTION, COFACTOR, SUBCELLULAR
RP   LOCATION, AND VARIANT LYS-396.
RX   PubMed=10224084; DOI=10.1074/jbc.274.19.13250;
RA   Vande Weghe J.G., Ow D.W.;
RT   "A fission yeast gene for mitochondrial sulfide oxidation.";
RL   J. Biol. Chem. 274:13250-13257(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Mutoh N., Kawabata M., Nakagawa C., Yamada K.;
RT   "Molecular cloning of the gene involved in cadmium sensitivity of fission
RT   yeast Schizosaccharomyces pombe.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of
CC       a quinone. {ECO:0000269|PubMed:10224084}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:10224084};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10224084};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10224084}.
CC   -!- SIMILARITY: Belongs to the SQRD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA22793.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA22793.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AF042283; AAD41159.1; -; Genomic_DNA.
DR   EMBL; AB007905; BAA22793.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU329671; CAA21882.1; -; Genomic_DNA.
DR   PIR; T43278; T43278.
DR   PIR; T43558; T43558.
DR   RefSeq; NP_596067.1; NM_001021978.2.
DR   AlphaFoldDB; O94284; -.
DR   SMR; O94284; -.
DR   BioGRID; 276856; 86.
DR   STRING; 4896.SPBC2G5.06c.1; -.
DR   iPTMnet; O94284; -.
DR   MaxQB; O94284; -.
DR   PaxDb; O94284; -.
DR   PRIDE; O94284; -.
DR   EnsemblFungi; SPBC2G5.06c.1; SPBC2G5.06c.1:pep; SPBC2G5.06c.
DR   GeneID; 2540326; -.
DR   KEGG; spo:SPBC2G5.06c; -.
DR   PomBase; SPBC2G5.06c; hmt2.
DR   VEuPathDB; FungiDB:SPBC2G5.06c; -.
DR   eggNOG; KOG3851; Eukaryota.
DR   HOGENOM; CLU_030742_2_2_1; -.
DR   InParanoid; O94284; -.
DR   OMA; FPWVYYN; -.
DR   PhylomeDB; O94284; -.
DR   BRENDA; 1.8.5.4; 5613.
DR   PRO; PR:O94284; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR   GO; GO:0071949; F:FAD binding; IDA:PomBase.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0070224; F:sulfide:quinone oxidoreductase activity; IDA:PomBase.
DR   GO; GO:0098849; P:cellular detoxification of cadmium ion; IMP:PomBase.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IMP:PomBase.
DR   GO; GO:0070219; P:cellular sulfide ion homeostasis; IMP:PomBase.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IMP:PomBase.
DR   GO; GO:0046938; P:phytochelatin biosynthetic process; IMP:PomBase.
DR   GO; GO:0042762; P:regulation of sulfur metabolic process; IMP:PomBase.
DR   GO; GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR015904; Sulphide_quinone_reductase.
DR   PANTHER; PTHR10632; PTHR10632; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   Cadmium; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Quinone;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..459
FT                   /note="Sulfide:quinone oxidoreductase, mitochondrial"
FT                   /id="PRO_0000021446"
FT   ACT_SITE        204
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7ZAG8"
FT   ACT_SITE        383
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7ZAG8"
FT   BINDING         35..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O67931"
FT   VARIANT         396
FT                   /note="E -> K (in cadmium sensitive strain)"
FT                   /evidence="ECO:0000269|PubMed:10224084"
SQ   SEQUENCE   459 AA;  51575 MW;  121F06DCC9579C04 CRC64;
     MLTLNSTIKS VTGSFQSASM LARFASTHHK VLVVGGGSAG ISVAHQIYNK FSKYRFANDQ
     GKDTSLKPGE IGIVDGAKYH YYQPGWTLTG AGLSSVAKTR RELASLVPAD KFKLHPEFVK
     SLHPRENKIV TQSGQEISYD YLVMAAGIYT DFGRIKGLTE ALDDPNTPVV TIYSEKYADA
     VYPWIEKTKS GNAIFTQPSG VLKCAGAPQK IMWMAEDYWR RHKVRSNIDV SFYTGMPTLF
     SVKRYSDALL RQNEQLHRNV KINYKDELVE VKGSERKAVF KNLNDGSLFE RPFDLLHAVP
     SMRSHEFIAK SDLADKSGFV AVDQSTTQST KFPNVFAIGD CSGLPTSKTY AAITAQAPVM
     VHNLWSFVNG KNLTASYNGY TSCPLLTGYG KLILAEFLYK QEPKESFGRF SRFLDQTVPR
     RMFYHLKKDF FPFVYWNFAV RNGKWYGSRG LIPPHFPVN
 
 
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