ID A0A410GC93_9BURK Unreviewed; 249 AA.
AC A0A410GC93;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN ORFNames=CKA81_08660 {ECO:0000313|EMBL:QAA93900.1};
OS Pollutimonas thiosulfatoxidans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=2028345 {ECO:0000313|EMBL:QAA93900.1, ECO:0000313|Proteomes:UP000283474};
RN [1] {ECO:0000313|EMBL:QAA93900.1, ECO:0000313|Proteomes:UP000283474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ye3 {ECO:0000313|Proteomes:UP000283474};
RA Park S.-J., Kim H.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
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_02087,
CC ECO:0000256|RuleBase:RU004514}.
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DR EMBL; CP022987; QAA93900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410GC93; -.
DR KEGG; pus:CKA81_08660; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000283474; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR CDD; cd00635; PLPDE_III_YBL036c_like; 1.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283474}.
FT DOMAIN 11..233
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 249 AA; 27724 MW; 5216DAA016186A46 CRC64;
MTEDSSIAAR LAQIQQRISQ AAVRAGRAAD AVRLLPVSKT FGEAAIREAV QAGVRRFGEN
KAQEIRSKYE PLADCDIEWI MIGHLQTNKA KDVARMAAEI QSLDRIELAI ALEKRLQQEG
RQIDALVQIK TSTEPTKYGL PPGELPDFLR RVADEAPSLR IQGLMTLAIN EANDEAVRAC
FRNLRELRDR TRDLDLPGVQ LDRLSMGMSG DFEIAIEEGS TEVRIGTAIF GGRVYNDDYY
WPEGVKKAP
//
