ID   A0A1J0VGB2_9GAMM        Unreviewed;       234 AA.
AC   A0A1J0VGB2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BOX17_08795 {ECO:0000313|EMBL:APE31042.1};
OS   Halomonas aestuarii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE31042.1, ECO:0000313|Proteomes:UP000181985};
RN   [1] {ECO:0000313|Proteomes:UP000181985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA   Koh H.-W., Rani S., Park S.-J.;
RT   "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated
RT   from solar salt.";
RL   Submitted (NOV-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}.
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; CP018139; APE31042.1; -; Genomic_DNA.
DR   RefSeq; WP_071943713.1; NZ_CP018139.1.
DR   AlphaFoldDB; A0A1J0VGB2; -.
DR   KEGG; hsi:BOX17_08795; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000181985; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06824; PLPDE_III_Yggs_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          10..231
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         38
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   234 AA;  25780 MW;  DDC61FF674BC21D3 CRC64;
     MTDLVLSESL TAVRARLEEA LRAAGRPADD ARLLAVSKTK PAELIREAWH EGQREFGENY
     VQEALDKQAE LADLDPIVWH FIGPLQSNKT RDVAEHFSWV HSVDRERIAR RLNDQRPEAL
     GPLDICLQVN ISDEASKSGL SLDELPALAE AVLSMPRLRL RGLMAIPAPA EGLAAQRAPF
     ARLREALEGL RERFPEAPLD TLSMGMSDDL EAAVLEGATL VRLGTAIFGA RAHR
//