ID L0AXA0_THEEQ Unreviewed; 231 AA.
AC L0AXA0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
DE Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
GN ORFNames=BEWA_023680 {ECO:0000313|EMBL:AFZ79519.1};
OS Theileria equi strain WA.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ79519.1, ECO:0000313|Proteomes:UP000031512};
RN [1] {ECO:0000313|EMBL:AFZ79519.1, ECO:0000313|Proteomes:UP000031512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA {ECO:0000313|EMBL:AFZ79519.1,
RC ECO:0000313|Proteomes:UP000031512};
RX PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT "Comparative genomic analysis and phylogenetic position of Theileria
RT equi.";
RL BMC Genomics 13:603-603(2012).
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:0000256|HAMAP-
CC Rule:MF_03225}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_03225,
CC ECO:0000256|RuleBase:RU004514}.
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DR EMBL; CP001669; AFZ79519.1; -; Genomic_DNA.
DR RefSeq; XP_004829185.1; XM_004829128.1.
DR AlphaFoldDB; L0AXA0; -.
DR STRING; 1537102.L0AXA0; -.
DR EnsemblProtists; AFZ79519; AFZ79519; BEWA_023680.
DR GeneID; 15806189; -.
DR KEGG; beq:BEWA_023680; -.
DR VEuPathDB; PiroplasmaDB:BEWA_023680; -.
DR eggNOG; KOG3157; Eukaryota.
DR OrthoDB; 21261at2759; -.
DR Proteomes; UP000031512; Chromosome 1.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS01211; UPF0001; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03225,
KW ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031512}.
FT DOMAIN 48..229
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03225,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 231 AA; 25880 MW; FA06112BE7507F86 CRC64;
MEDENPKTED ATSIEDEMRP ILAAWRSISE YCRVRNVDVL IASKGRSTEA ISALYRAGQT
HFGENRVDEL VAKAQELDNL PIKWHFIGHL QSNKCKMLAS VKGLYMVESI DSVKTAMELD
KCLERVSKTV KVLVQVNTTL REQFGILYNQ MEKVREVVSA VLASQHLEFS GLMTIGDGTS
ECYARLISVR SELERSVGPC KVMSMGMSHD WKDAIEGGST QVRVGRCLFE A
//
