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YF19_SCHPO
ID   YF19_SCHPO              Reviewed;         503 AA.
AC   O14293; P78895;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Putative aldehyde dehydrogenase-like protein C9E9.09c;
DE            EC=1.2.1.-;
GN   ORFNames=SPAC9E9.09c;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-503.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-501, AND
RP   IDENTIFICATION BY 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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB16407.1; -; Genomic_DNA.
DR   EMBL; D89246; BAA13907.1; -; mRNA.
DR   PIR; T39216; T39216.
DR   PIR; T43153; T43153.
DR   RefSeq; NP_594582.1; NM_001020011.2.
DR   AlphaFoldDB; O14293; -.
DR   SMR; O14293; -.
DR   BioGRID; 279414; 74.
DR   STRING; 4896.SPAC9E9.09c.1; -.
DR   iPTMnet; O14293; -.
DR   MaxQB; O14293; -.
DR   PaxDb; O14293; -.
DR   PRIDE; O14293; -.
DR   EnsemblFungi; SPAC9E9.09c.1; SPAC9E9.09c.1:pep; SPAC9E9.09c.
DR   GeneID; 2542976; -.
DR   KEGG; spo:SPAC9E9.09c; -.
DR   PomBase; SPAC9E9.09c; -.
DR   VEuPathDB; FungiDB:SPAC9E9.09c; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_0_1; -.
DR   InParanoid; O14293; -.
DR   OMA; RKAFEKW; -.
DR   PhylomeDB; O14293; -.
DR   Reactome; R-SPO-196757; Metabolism of folate and pterines.
DR   Reactome; R-SPO-380612; Metabolism of serotonin.
DR   Reactome; R-SPO-5365859; RA biosynthesis pathway.
DR   Reactome; R-SPO-70350; Fructose catabolism.
DR   Reactome; R-SPO-71384; Ethanol oxidation.
DR   PRO; PR:O14293; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:PomBase.
DR   GO; GO:0019413; P:acetate biosynthetic process; ISO:PomBase.
DR   GO; GO:0006068; P:ethanol catabolic process; ISS:PomBase.
DR   GO; GO:0006740; P:NADPH regeneration; ISO:PomBase.
DR   GO; GO:0006090; P:pyruvate metabolic process; ISO:PomBase.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..503
FT                   /note="Putative aldehyde dehydrogenase-like protein
FT                   C9E9.09c"
FT                   /id="PRO_0000056595"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        304
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         247..252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            171
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        378
FT                   /note="N -> Y (in Ref. 2; BAA13907)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  54768 MW;  A7787A2181FB9CD5 CRC64;
     MSTKLVDHVE ITVPTGKTYI QPVGLFINNQ HVDSVHGGRV KVYSPSTEKL ICEVADADEE
     DVDIAVKVAR AAFQTDAPWR KFSSAQRGRC LSRLADCIEQ NLEYLASIET LDNGKSITLA
     RGDVQAAADC FRYYGGWADK DYGQTIETDI KRFAYTRHEP IGVCGQIIPW NFPFLMCAWK
     IAPAVACGNT IILKTAELTP LSALCLTKFV PECGFPPGVI NVLSGDGRRC GNAISSHMDI
     DKVAFTGSTG VGRMVMRAAA SSNLKKVTLE LGGKSPNIVF NDADLDSAAV WTNYGIFYNS
     GQVCCAGSRV YVQEDVYDEF IKRMVAKAKT LKVGDPFAED TFQGAQVSKQ QYERIVSYIE
     SGIAHGAKLE IGGKRHGNLG YFVEPTILSN VTEDMAVGKE EIFGPVLAVI KFKTIEEAIR
     RGNNSTYGLA AGVHTNNITN AIKVSNALEA GTVWVNCYNL LHHQIPFGGY KESGIGRELG
     SYGLTNYTQT KAVHINLGMD SPI
 
 
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