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PLPHP_PONAB
ID   PLPHP_PONAB             Reviewed;         275 AA.
AC   Q5R4Z1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE            Short=PLP homeostasis protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE   AltName: Full=Proline synthase co-transcribed bacterial homolog protein {ECO:0000255|HAMAP-Rule:MF_03225};
DE   AltName: Full=Pyridoxal phosphate-binding protein {ECO:0000250|UniProtKB:O94903};
GN   Name=PLPBP {ECO:0000255|HAMAP-Rule:MF_03225};
GN   Synonyms=PROSC {ECO:0000255|HAMAP-Rule:MF_03225};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000255|HAMAP-Rule:MF_03225}.
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DR   EMBL; CR861096; CAH93175.1; -; mRNA.
DR   RefSeq; NP_001126869.1; NM_001133397.1.
DR   AlphaFoldDB; Q5R4Z1; -.
DR   SMR; Q5R4Z1; -.
DR   STRING; 9601.ENSPPYP00000020750; -.
DR   GeneID; 100173881; -.
DR   KEGG; pon:100173881; -.
DR   CTD; 11212; -.
DR   eggNOG; KOG3157; Eukaryota.
DR   InParanoid; Q5R4Z1; -.
DR   OrthoDB; 1423577at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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.
DR   PROSITE; PS01211; UPF0001; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..275
FT                   /note="Pyridoxal phosphate homeostasis protein"
FT                   /id="PRO_0000249597"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94903"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03225"
FT   MOD_RES         69
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2Y8"
FT   MOD_RES         125
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2Y8"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94903"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94903"
SQ   SEQUENCE   275 AA;  30179 MW;  931EE7159DDC7653 CRC64;
     MWRAGSMSAE LGVGCALRAV NERVQQAVAL RPRDLPAIQP RLVAVSKTKP ADMVIEAYGH
     GQRTFGENYV QELLEKASNP KILSLGPEIK WHFIGHLQKQ NVNKLMAVPN LFVLETVDSV
     KLAGKVNSSW QKKGSPERLK VMVQINTSGE ESKHGLPPSE TIAIVEHINA KCPNLEFVGL
     MTIGSFGHDL SQGPNPDFQL LLSLREELCK KLNIPADQVE LSMGMSVDFQ HAIEVGSTNV
     RIGSMIFGER DYSKKPAPDK CAADVKAPLE VAQEH
 
 
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