GenomeNet

Database: UniProt
Entry: D4LBS0_RUMC1
LinkDB: D4LBS0_RUMC1
Original site: D4LBS0_RUMC1 
ID   D4LBS0_RUMC1            Unreviewed;       229 AA.
AC   D4LBS0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   OrderedLocusNames=RUM_08890 {ECO:0000313|EMBL:CBL17065.1};
OS   Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS   18P13).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL17065.1, ECO:0000313|Proteomes:UP000007054};
RN   [1] {ECO:0000313|Proteomes:UP000007054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18848 / JCM 17042 / 18P13
RC   {ECO:0000313|Proteomes:UP000007054};
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Ruminococcus sp. 18P13.";
RL   Submitted (MAR-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   ---------------------------------------------------------------------------
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; FP929052; CBL17065.1; -; Genomic_DNA.
DR   RefSeq; WP_015557972.1; NC_021039.1.
DR   AlphaFoldDB; D4LBS0; -.
DR   STRING; 213810.RUM_08890; -.
DR   GeneID; 83155662; -.
DR   KEGG; rch:RUM_08890; -.
DR   PATRIC; fig|213810.4.peg.801; -.
DR   HOGENOM; CLU_059988_1_0_9; -.
DR   BioCyc; RCHA213810:RUM_RS04290-MONOMER; -.
DR   Proteomes; UP000007054; 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:UP000007054}.
FT   DOMAIN          19..228
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   229 AA;  25708 MW;  1DF98A362A2FE7A9 CRC64;
     MERSAEQVRE NYKRITDRIG EAMAKYRKPE EQVQLMAVTK TVDPALVNVA VECGVRLLGE
     NRVQEYESKK AQYDPRAQVQ FIGQLQTNKV KYLIPEISMI QSVDSLHLAN EVERIAARAD
     KVQDILLEVN IGGEESKGGI PAEELHGLLE EAARKPHLHV CGLMTIPPKT DVEKYFFRMQ
     KLFIDISAEN MDNIDMHVLS MGMSGDYVEA IKYGSTLVRI GSALFGARG
//
DBGET integrated database retrieval system