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Database: UniProt
Entry: A0A1W6WD50_9FIRM
LinkDB: A0A1W6WD50_9FIRM
Original site: A0A1W6WD50_9FIRM 
ID   A0A1W6WD50_9FIRM        Unreviewed;       248 AA.
AC   A0A1W6WD50;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=B6259_04340 {ECO:0000313|EMBL:ARP50175.1};
OS   Ruminococcaceae bacterium CPB6.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=1572656 {ECO:0000313|EMBL:ARP50175.1, ECO:0000313|Proteomes:UP000195433};
RN   [1] {ECO:0000313|EMBL:ARP50175.1, ECO:0000313|Proteomes:UP000195433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPB6 {ECO:0000313|EMBL:ARP50175.1,
RC   ECO:0000313|Proteomes:UP000195433};
RA   Tao Y.;
RT   "Complete genome sequence of Ruminococcaceae bacterial strain CPB6.";
RL   Submitted (APR-2017) 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; CP020705; ARP50175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6WD50; -.
DR   STRING; 1572656.B6259_04340; -.
DR   KEGG; rbp:B6259_04340; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000195433; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195433}.
FT   DOMAIN          26..243
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   COILED          8..35
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         50
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   248 AA;  27694 MW;  8A01ADBB280DF8B2 CRC64;
     MTTKSLSEED LQRRFRDVEE NLKVVEERIA AAAEHAGRKR EDITLLAATK TVPVEIINHG
     IEAGIRCIGE NRVQELMDKY EGYRKDLADV QFIGHLQTNK VKYLIGKVSL IQSIDSRKLA
     AEVSRLSQRA GITTNILLEV NIGREENKSG VLPENLEQLL GEVSQMPNIQ VRGLMAIPPA
     GAEKEETFAY FTQMYQYFID IGSKKLDNVS MQRLSMGMSA DYELAIAAGA NMVRVGSALF
     GPRDYSKK
//
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