ID   A0A136N5Z5_9BACT        Unreviewed;       242 AA.
AC   A0A136N5Z5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=UZ11_BCD004001870 {ECO:0000313|EMBL:KXK41589.1};
OS   Bacteroidetes bacterium OLB11.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617422 {ECO:0000313|EMBL:KXK41589.1, ECO:0000313|Proteomes:UP000070496};
RN   [1] {ECO:0000313|EMBL:KXK41589.1, ECO:0000313|Proteomes:UP000070496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB11 {ECO:0000313|EMBL:KXK41589.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK41589.1}.
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DR   EMBL; LNFQ01000062; KXK41589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136N5Z5; -.
DR   STRING; 1617422.UZ11_BCD004001870; -.
DR   PATRIC; fig|1617422.3.peg.2035; -.
DR   Proteomes; UP000070496; 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          43..229
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   242 AA;  27863 MW;  1713AA5D519AD154 CRC64;
     MDEIVSHIAQ IKNRINQTCK KIGRNPDEVQ LILATKTVSP ERIKIAIESG EKCIAENKVQ
     ELKEKYDALK DTPHINHFIG HLQSNKIKDI LKYDVRCVQS IDRLELAEKL HKRLLIEKKE
     IDILIQVNTS FEKSKFGIEP NETMNLIKKI SQFSTLKIKG LMTIGLFSTE AEQVRKCFRL
     LKSIQEEIIN EQIPNVEMKE LSMGMSGDLE TAIEEGATIV RVGTAIFGKR IYSDSYYWNE
     YH
//