ID   PLPHP_SCHPO             Reviewed;         237 AA.
AC   Q9P6Q1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE            Short=PLP homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
GN   ORFNames=SPAC644.09;
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: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be
CC       involved in intracellular homeostatic regulation of pyridoxal 5'-
CC       phosphate (PLP), the active form of vitamin B6. {ECO:0000255|HAMAP-
CC       Rule:MF_03225}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000255|HAMAP-Rule:MF_03225}.
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DR   EMBL; CU329670; CAB90136.1; -; Genomic_DNA.
DR   RefSeq; NP_593877.1; NM_001019307.2.
DR   AlphaFoldDB; Q9P6Q1; -.
DR   SMR; Q9P6Q1; -.
DR   BioGRID; 280072; 15.
DR   STRING; 4896.SPAC644.09.1; -.
DR   MaxQB; Q9P6Q1; -.
DR   PaxDb; Q9P6Q1; -.
DR   EnsemblFungi; SPAC644.09.1; SPAC644.09.1:pep; SPAC644.09.
DR   GeneID; 2543658; -.
DR   KEGG; spo:SPAC644.09; -.
DR   PomBase; SPAC644.09; -.
DR   VEuPathDB; FungiDB:SPAC644.09; -.
DR   eggNOG; KOG3157; Eukaryota.
DR   HOGENOM; CLU_059988_2_0_1; -.
DR   InParanoid; Q9P6Q1; -.
DR   OMA; IEWHMIG; -.
DR   PhylomeDB; Q9P6Q1; -.
DR   PRO; PR:Q9P6Q1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISO:PomBase.
DR   GO; GO:0042816; P:vitamin B6 metabolic process; ISS:PomBase.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_02087; PLP_homeostasis; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011078; PyrdxlP_homeostasis.
DR   PANTHER; PTHR10146; PTHR10146; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00044; TIGR00044; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..237
FT                   /note="Pyridoxal phosphate homeostasis protein"
FT                   /id="PRO_0000316622"
FT   MOD_RES         31
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03225"
SQ   SEQUENCE   237 AA;  26393 MW;  0E768E0E9A63ED2E CRC64;
     MSTIHSCLDL IRSQIQQSAN GRNVLLVAVS KFHPVETLME AYNAGQRHFG ENYMQEFLKK
     VELMPDDVQW HFIGSLQSSK CKKIASVKNL YSIETIDTEK KARLVNSARE ALQLPLNVYI
     QVNTSGEENK GGVTPSKVLE LCKQVQDMKY LRLKGLMTIG SISNSQLSDH NPDFQVLSDL
     RESLQNELGI PLQLSMGMSS DYLLAIKYGS DSVRVGSSIF GSRPTEKPSD VHISASK