ID   PLR2_SCHPO              Reviewed;         333 AA.
AC   O94521;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Probable pyridoxal reductase 2;
DE            Short=PL reductase 2;
DE            Short=PL-red 2;
DE            EC=1.1.1.65;
GN   ORFNames=SPCC1281.04;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22825.1; -; Genomic_DNA.
DR   PIR; T40923; T40923.
DR   RefSeq; NP_588168.1; NM_001023157.2.
DR   AlphaFoldDB; O94521; -.
DR   SMR; O94521; -.
DR   BioGRID; 275736; 17.
DR   STRING; 4896.SPCC1281.04.1; -.
DR   MaxQB; O94521; -.
DR   PaxDb; O94521; -.
DR   EnsemblFungi; SPCC1281.04.1; SPCC1281.04.1:pep; SPCC1281.04.
DR   GeneID; 2539165; -.
DR   KEGG; spo:SPCC1281.04; -.
DR   PomBase; SPCC1281.04; -.
DR   VEuPathDB; FungiDB:SPCC1281.04; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   HOGENOM; CLU_023205_2_1_1; -.
DR   InParanoid; O94521; -.
DR   OMA; QFKKFDD; -.
DR   PhylomeDB; O94521; -.
DR   PRO; PR:O94521; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; ISO:PomBase.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0050236; F:pyridoxine:NADP 4-dehydrogenase activity; ISS:PomBase.
DR   GO; GO:0042821; P:pyridoxal biosynthetic process; ISS:PomBase.
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   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..333
FT                   /note="Probable pyridoxal reductase 2"
FT                   /id="PRO_0000310315"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36844 MW;  D69C0BEE8735E0F2 CRC64;
     MPIVNGFKVG PIGLGLMGLT WRPKQTPIKQ AFELMNYALS QGSNYWNAGE FYGINPPTAN
     LDLLADYFEK YPKNADKVFL SVKGGTDFKT LAPHGDPESV TKSVKNALTR LRGKKKLDLF
     QCARVDHKVP IETTMKALKA FVDSGEISCV GLSEASAESI KRALAIVPIA AVETEYSLFS
     RDIEKNGILD TCTQLSIPII AYAPFCHGLL TGRVKTAEDL KDFIKAFPFL RNMDKFNPKV
     FEKNIPFLKA VEQLAQKFGM SMPEFALNFI IANGKGMIIP IPGSTTVQRA ESNLSALKKS
     LSSEQLEEAK KVLDKHQIFG LRYNKQLEST LSI