GenomeNet

Database: UniProt
Entry: W5Y387_9CORY
LinkDB: W5Y387_9CORY
Original site: W5Y387_9CORY 
ID   W5Y387_9CORY            Unreviewed;       244 AA.
AC   W5Y387;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=B843_09725 {ECO:0000313|EMBL:AHI23330.1};
OS   Corynebacterium vitaeruminis DSM 20294.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI23330.1, ECO:0000313|Proteomes:UP000019222};
RN   [1] {ECO:0000313|EMBL:AHI23330.1, ECO:0000313|Proteomes:UP000019222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL   Submitted (FEB-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}.
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; CP004353; AHI23330.1; -; Genomic_DNA.
DR   RefSeq; WP_025253341.1; NZ_CP004353.1.
DR   AlphaFoldDB; W5Y387; -.
DR   STRING; 1224164.B843_09725; -.
DR   KEGG; cvt:B843_09725; -.
DR   PATRIC; fig|1224164.3.peg.1965; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_1_0_11; -.
DR   Proteomes; UP000019222; Chromosome.
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:UP000019222}.
FT   DOMAIN          27..237
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   244 AA;  26980 MW;  0CADF196C7DBDAEE CRC64;
     MTDPNFHPET VEQFREAHEA VLARMADAAR RAGRSPEEVR LIAVSKTNPI ERVRLAVEAG
     MTLLGENRPQ ELAEKAEAIP GVTWCAIGHL QRNKAREVAR YAHEFHALDS LRLAQALQSR
     LETEDRTLDV FIQVNASHEG QKSGFGAADV APFLEDLAGL DRLRLRGLMT MAAFDAPEQV
     IRGSFAELRE LRDRLQGSLP DGMTCQELSM GMTGDFEWAI EEGATSVRVG TAIFGHRANS
     AYLK
//
DBGET integrated database retrieval system