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Database: UniProt
Entry: A0A117LD20_9BACT
LinkDB: A0A117LD20_9BACT
Original site: A0A117LD20_9BACT 
ID   A0A117LD20_9BACT        Unreviewed;       238 AA.
AC   A0A117LD20;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 21.
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=XD68_1189 {ECO:0000313|EMBL:KUK39248.1};
OS   Synergistales bacterium 54_24.
OC   Bacteria; Synergistota; Synergistia; Synergistales.
OX   NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK39248.1, ECO:0000313|Proteomes:UP000054050};
RN   [1] {ECO:0000313|Proteomes:UP000054050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK39248.1}.
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DR   EMBL; LGFQ01000056; KUK39248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117LD20; -.
DR   STRING; 1635272.XD68_1189; -.
DR   PATRIC; fig|1635272.3.peg.1231; -.
DR   Proteomes; UP000054050; 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          13..229
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   238 AA;  26059 MW;  A809D221CC43C18B CRC64;
     MVGSNADIKE RVNAVRERIA LAAQRVGRKP HEVRLVAVSK GRGVEEMIEA VRAGVDAIGE
     NRVQEAAQKR ALWPASMAVP WHMVGHLQRN KASKALDLFD IIQSVDSIPL ADALSHLAAQ
     KGKTLPIFLE VNASREGSKY GFPPEEAVNA AEAVAELSNL RLLGLMTIGP LTDDRAQVRG
     AFGLLRELRD KINETLKLGL SELSMGMSDD FETAVEEGST MVRIGRAIFD LKKRPFER
//
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