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