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SOU1_SCHPO
ID   SOU1_SCHPO              Reviewed;         255 AA.
AC   Q9Y6Z9;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Sorbose reductase sou1;
DE            EC=1.1.1.289;
DE   AltName: Full=Sorbitol utilization protein sou1;
GN   Name=sou1; ORFNames=SPAC8E11.10;
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).
CC   -!- FUNCTION: Catalyzes the NADP dependent reduction of L-sorbose to D-
CC       glucitol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH;
CC         Xref=Rhea:RHEA:14609, ChEBI:CHEBI:13172, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17924, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.289;
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB40197.1; -; Genomic_DNA.
DR   PIR; T39164; T39164.
DR   RefSeq; NP_594161.1; NM_001019585.2.
DR   AlphaFoldDB; Q9Y6Z9; -.
DR   SMR; Q9Y6Z9; -.
DR   BioGRID; 279848; 1.
DR   STRING; 4896.SPAC8E11.10.1; -.
DR   iPTMnet; Q9Y6Z9; -.
DR   MaxQB; Q9Y6Z9; -.
DR   PaxDb; Q9Y6Z9; -.
DR   PRIDE; Q9Y6Z9; -.
DR   EnsemblFungi; SPAC8E11.10.1; SPAC8E11.10.1:pep; SPAC8E11.10.
DR   GeneID; 2543428; -.
DR   KEGG; spo:SPAC8E11.10; -.
DR   PomBase; SPAC8E11.10; -.
DR   VEuPathDB; FungiDB:SPAC8E11.10; -.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_1_1_1; -.
DR   InParanoid; Q9Y6Z9; -.
DR   OMA; YKCSVQN; -.
DR   PhylomeDB; Q9Y6Z9; -.
DR   PRO; PR:Q9Y6Z9; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0032115; F:sorbose reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..255
FT                   /note="Sorbose reductase sou1"
FT                   /id="PRO_0000054777"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   255 AA;  27437 MW;  8609CDC5B9698544 CRC64;
     MTSMFSLKGK TTLITGGSGG IGFSIAKAFA AAGSNVGLLY GRNKKALEYA AELRDKHGVQ
     AKAYSCPIEN RSAVIETTNQ AVEELGGRLD VMIANAGIAI PHLSLEDKNE DIWTKVVGIN
     LNGAYYTAQA AGHHFKKQGK GSLIFTASMS GHIANWPQQW ASYHATKAAV KHLARALAVE
     WAPFARVNSV SPGYIDTDLT LYADENLRKK WKEYTPQARI GLPDELPGAY LYLASDASSY
     CTGSDIIVDG GYCSR
 
 
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