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Database: UniProt
Entry: A0A0B5D3Q0_9CORY
LinkDB: A0A0B5D3Q0_9CORY
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ID   A0A0B5D3Q0_9CORY        Unreviewed;       230 AA.
AC   A0A0B5D3Q0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=B842_08705 {ECO:0000313|EMBL:AJE33590.1};
OS   Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE33590.1, ECO:0000313|Proteomes:UP000031524};
RN   [1] {ECO:0000313|EMBL:AJE33590.1, ECO:0000313|Proteomes:UP000031524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT   isolated from a wastewater-fed microbial fuel cell.";
RL   Submitted (APR-2013) 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; CP005286; AJE33590.1; -; Genomic_DNA.
DR   RefSeq; WP_040086214.1; NZ_CP005286.1.
DR   AlphaFoldDB; A0A0B5D3Q0; -.
DR   STRING; 1223515.B842_08705; -.
DR   KEGG; chm:B842_08705; -.
DR   HOGENOM; CLU_059988_0_0_11; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000031524; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
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          10..228
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   230 AA;  24468 MW;  E507AADD5C4F0213 CRC64;
     MTRLEELRTN LTAVRERIDA AARAADRDPA DIRLLPVTKF HPASDLELLV ELGVADVAEN
     REQEARAKAA EVPDARIHMI GQIQTKKANS VARWAASVHS LDSVRLAEGL NRGMGLAIER
     GDRPAGVLPV YLQLSADGDP SRGGVTEENL QELVDVVEAA PHLELRGLMV VPPLGEDPGP
     VFAWARTLCD DLGPGMELSA GMSADLESAV AKGSNIVRVG TGVLGSRPLP
//
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