PLR1_YEAST
ID PLR1_YEAST Reviewed; 345 AA.
AC Q06494; D6W4C4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Putative pyridoxal reductase;
DE Short=PL reductase;
DE Short=PL-red;
DE EC=1.1.1.65;
GN OrderedLocusNames=YPR127W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Catalyzes the reduction of pyridoxal (PL) with NADPH and
CC oxidation of pyridoxine (PN) with NADP(+). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal;
CC Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65;
CC -!- PATHWAY: Cofactor degradation; B6 vitamer degradation; pyridoxal from
CC pyridoxine (dehydrogenase route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; U40828; AAB68066.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11540.1; -; Genomic_DNA.
DR PIR; S69018; S69018.
DR RefSeq; NP_015452.1; NM_001184224.1.
DR AlphaFoldDB; Q06494; -.
DR SMR; Q06494; -.
DR BioGRID; 36294; 31.
DR IntAct; Q06494; 1.
DR STRING; 4932.YPR127W; -.
DR iPTMnet; Q06494; -.
DR MaxQB; Q06494; -.
DR PaxDb; Q06494; -.
DR PRIDE; Q06494; -.
DR EnsemblFungi; YPR127W_mRNA; YPR127W; YPR127W.
DR GeneID; 856245; -.
DR KEGG; sce:YPR127W; -.
DR SGD; S000006331; YPR127W.
DR VEuPathDB; FungiDB:YPR127W; -.
DR eggNOG; KOG1575; Eukaryota.
DR HOGENOM; CLU_023205_2_1_1; -.
DR InParanoid; Q06494; -.
DR OMA; MTMAYGA; -.
DR BioCyc; MetaCyc:G3O-34264-MON; -.
DR BioCyc; YEAST:G3O-34264-MON; -.
DR UniPathway; UPA00192; UER00307.
DR PRO; PR:Q06494; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06494; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0050236; F:pyridoxine:NADP 4-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042820; P:vitamin B6 catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="Putative pyridoxal reductase"
FT /id="PRO_0000257816"
FT ACT_SITE 60
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 38601 MW; C443ED79F25EA106 CRC64;
MSVADLKNNI HKLDTGYGLM SLTWRAEPIP QSQAFEAMHR VVELSRERGH KAFFNVGEFY
GPDFINLSYV HDFFAKYPDL RKDVVISCKG GADNATLTPR GSHDDVVQSV KNSVSAIGGY
IDIFEVARID TSLCTKGEVY PYESFEALAE MISEGVIGGI SLSEVNEEQI RAIHKDWGKF
LTCVEVELSL FSNDILHNGI AKTCAELGLS IICYSPLGRG LLTGQLKSNA DIPEGDFRKS
LKRFSDESLK KNLTLVRFLQ EEIVDKRPQN NSITLAQLAL GWVKHWNKVP EYSGAKFIPI
PSGSSISKVN ENFDEQKTKL TDQEFNAINK YLTTFHTVGD RYEMA
