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Database: UniProt
Entry: E0DGJ7_9CORY
LinkDB: E0DGJ7_9CORY
Original site: E0DGJ7_9CORY 
ID   E0DGJ7_9CORY            Unreviewed;       246 AA.
AC   E0DGJ7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=HMPREF0299_6995 {ECO:0000313|EMBL:EFM48765.1};
OS   Corynebacterium matruchotii ATCC 14266.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM48765.1, ECO:0000313|Proteomes:UP000004218};
RN   [1] {ECO:0000313|EMBL:EFM48765.1, ECO:0000313|Proteomes:UP000004218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM48765.1,
RC   ECO:0000313|Proteomes:UP000004218};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) 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:EFM48765.1}.
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DR   EMBL; ACSH02000005; EFM48765.1; -; Genomic_DNA.
DR   RefSeq; WP_005526030.1; NZ_ACSH02000005.1.
DR   AlphaFoldDB; E0DGJ7; -.
DR   STRING; 553207.HMPREF0299_6995; -.
DR   GeneID; 84574429; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000004218; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004218}.
FT   DOMAIN          17..241
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   246 AA;  26917 MW;  3E275900ABDFC278 CRC64;
     MPPYSTPSTV DEFRANYQAV TERIANAAHA AGRDPADIRL IAVSKTFPIS HALLAAEAGM
     TVLGENRPQE LAEKAQAFRI RGVDVTWCAI GHLQRNKAKE IAQFAAEFHA LDSLRLAEAL
     QHRLELANRT LDVFIQVNTS HESQKSGFAP DKVAAILPSL ATLDRLHVRG LMTMAAFSPE
     ESVVRPSFEQ LRTLRDRLQP DAPDGMSLTE LSMGMTGDFE WAIAEGATSV RIGTAIFGHR
     PNSAYL
//
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