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