PLPHP_CAEEL
ID PLPHP_CAEEL Reviewed; 244 AA.
AC P52057;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=F09E5.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; FO081044; CCD68760.1; -; Genomic_DNA.
DR PIR; T15996; T15996.
DR RefSeq; NP_495001.1; NM_062600.5.
DR AlphaFoldDB; P52057; -.
DR SMR; P52057; -.
DR BioGRID; 39251; 4.
DR STRING; 6239.F09E5.8; -.
DR EPD; P52057; -.
DR PaxDb; P52057; -.
DR PeptideAtlas; P52057; -.
DR EnsemblMetazoa; F09E5.8.1; F09E5.8.1; WBGene00017286.
DR GeneID; 173906; -.
DR KEGG; cel:CELE_F09E5.8; -.
DR UCSC; F09E5.8; c. elegans.
DR CTD; 173906; -.
DR WormBase; F09E5.8; CE02615; WBGene00017286; -.
DR eggNOG; KOG3157; Eukaryota.
DR GeneTree; ENSGT00390000004928; -.
DR HOGENOM; CLU_059988_2_1_1; -.
DR InParanoid; P52057; -.
DR OMA; IEWHMIG; -.
DR OrthoDB; 1423577at2759; -.
DR PhylomeDB; P52057; -.
DR PRO; PR:P52057; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017286; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
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 3: Inferred from homology;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..244
FT /note="Pyridoxal phosphate homeostasis protein"
FT /id="PRO_0000163212"
FT MOD_RES 37
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03225"
SQ SEQUENCE 244 AA; 27196 MW; 4D6F3F3552A86A5A CRC64;
MSIEIVQKSL FNIIEAVADA VTASQATKRC RLVAVSKTKS ADLIEACYSQ NQRHFGENYV
QELEEKSDVL ASKCLDIRWH FIGQVQSNKI GKICNSPGLW CVETVETEKH ARIFDKEWSK
HGANLSPLRV LVQVNTSGED NKGGIEIGEA PKLAEFIRKE CQNLKFDGFM TIGSFDNSHA
SGENPDFEKL FKVRQTWAEQ TGESADSVEL SMGMSDDFLQ AIHQGATSVR VGSKLFGARE
YKNK