ID   A0A2S8W0N2_9CAUL        Unreviewed;       236 AA.
AC   A0A2S8W0N2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=CQ026_12160 {ECO:0000313|EMBL:PQZ78638.1};
OS   Brevundimonas sp. MYb31.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1848616 {ECO:0000313|EMBL:PQZ78638.1, ECO:0000313|Proteomes:UP000238612};
RN   [1] {ECO:0000313|EMBL:PQZ78638.1, ECO:0000313|Proteomes:UP000238612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb31 {ECO:0000313|EMBL:PQZ78638.1,
RC   ECO:0000313|Proteomes:UP000238612};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PQZ78638.1}.
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DR   EMBL; PCPM01000020; PQZ78638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8W0N2; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000238612; Unassembled WGS sequence.
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}.
FT   DOMAIN          49..228
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   236 AA;  24857 MW;  738CFE5AA9C444EF CRC64;
     MTASNPASVV PSIHDRFVAV RARIRSACVA AGGDPVSVVL TAVSKTQPDE ALEAALATGQ
     RVFGENRVQE AQAHWAGRRA AFPDLELRLI GPLQTNKAVE AVELFDVIET LDREKLAAAL
     AMAMQKTGRR PRVLVQVNTG AEPQKAGVLP EDADALIAAA RDGHGLNVEG VMCIPPADEA
     PEPHFKLLAE IAARNGLSVL SMGMSGDYET AIFSGATHVR VGSALFGERI APLKPS
//