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Database: UniProt
Entry: A0A160ILM0_9BACI
LinkDB: A0A160ILM0_9BACI
Original site: A0A160ILM0_9BACI 
ID   A0A160ILM0_9BACI        Unreviewed;       226 AA.
AC   A0A160ILM0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=ABE65_008235 {ECO:0000313|EMBL:ANC76786.1};
OS   Fictibacillus phosphorivorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC76786.1, ECO:0000313|Proteomes:UP000076623};
RN   [1] {ECO:0000313|EMBL:ANC76786.1, ECO:0000313|Proteomes:UP000076623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-29 {ECO:0000313|EMBL:ANC76786.1,
RC   ECO:0000313|Proteomes:UP000076623};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT   toxic to nematodes.";
RL   Submitted (APR-2016) 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; CP015378; ANC76786.1; -; Genomic_DNA.
DR   RefSeq; WP_066393471.1; NZ_CP015378.1.
DR   AlphaFoldDB; A0A160ILM0; -.
DR   STRING; 1221500.ABE65_008235; -.
DR   KEGG; fpn:ABE65_008235; -.
DR   Proteomes; UP000076623; 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.
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          25..223
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   226 AA;  25473 MW;  6A19ED217317AD0F CRC64;
     MGIKENKEYI LNEIQSACEK KNRSSKGVNL IAVTKYVSNE TTREAVLAGI EHIGENRIEG
     LLSKKEYLKD LPVKWHFIGT LQTRKVKDVI EHVDYIHSLD RLSLANEIQK RAVKTISCFV
     QVNVAEEDSK HGLPVKDVVA FVDKLKDYDS IKVVGLMTMA PFTEDESLIR NVFSTLKQLQ
     LEIQKQKMVH APCTELSMGM SNDYSIAVEE GATFIRVGTS LVGKEF
//
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