ID A0A7U6I689_9ENTE Unreviewed; 224 AA. AC A0A7U6I689; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 4. 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=EGX73_09635 {ECO:0000313|EMBL:AYY10085.1}; OS Enterococcus sp. FDAARGOS_553. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=2420313 {ECO:0000313|EMBL:AYY10085.1, ECO:0000313|Proteomes:UP000271079}; RN [1] {ECO:0000313|Proteomes:UP000271079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_553 {ECO:0000313|Proteomes:UP000271079}; RA Plongla R., Gilligan P., Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., RA Mehta A., Aluvathingal J., Nadendla S., Geyer C., Nandy P., Yan Y., RA Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (NOV-2018) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP033740; AYY10085.1; -; Genomic_DNA. DR RefSeq; WP_003127642.1; NZ_CP033740.1. DR AlphaFoldDB; A0A7U6I689; -. DR GeneID; 66474908; -. DR Proteomes; UP000271079; Chromosome. 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; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1. DR SUPFAM; SSF51419; PLP-binding barrel; 1. DR TIGRFAMs; TIGR00044; pyridoxal phosphate enzyme, YggS family; 1. DR PROSITE; PS01211; UPF0001; 1. PE 3: Inferred from homology; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087, KW ECO:0000256|PIRSR:PIRSR004848-1}. FT DOMAIN 12..222 FT /note="Ala_racemase_N" FT /evidence="ECO:0000259|Pfam:PF01168" FT MOD_RES 34 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087, FT ECO:0000256|PIRSR:PIRSR004848-1" SQ SEQUENCE 224 AA; 24930 MW; DD16FB13777F1E32 CRC64; MISENLHKIQ QEIQDSCALV SRKASEVRLV AVTKSVDSEK TRKIIEAGVT DCAENRVEKL LEKKQQLADF PEVNWHFIGN LQRRKVKSII NEVDYFHALE SLKLAQEIQK RAAKTIACFV EVNISGEASK QGIAPDDVVS FIEELQPFDK INVIGLMTMA PLASSEAEQL HYFHQLKELQ EKIAALHLAH APCTETSMGM SNDFAVAIQA GATVVRIGTA LFQE //