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Database: UniProt
Entry: A0A087ARF7_9BIFI
LinkDB: A0A087ARF7_9BIFI
Original site: A0A087ARF7_9BIFI 
ID   A0A087ARF7_9BIFI        Unreviewed;       277 AA.
AC   A0A087ARF7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=BIGA_0805 {ECO:0000313|EMBL:KFI61357.1};
OS   Bifidobacterium pullorum subsp. gallinarum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI61357.1, ECO:0000313|Proteomes:UP000029046};
RN   [1] {ECO:0000313|EMBL:KFI61357.1, ECO:0000313|Proteomes:UP000029046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI61357.1,
RC   ECO:0000313|Proteomes:UP000029046};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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:KFI61357.1}.
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DR   EMBL; JGYX01000002; KFI61357.1; -; Genomic_DNA.
DR   RefSeq; WP_033507151.1; NZ_JGYX01000002.1.
DR   AlphaFoldDB; A0A087ARF7; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000029046; 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:UP000029046}.
FT   DOMAIN          40..274
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         55
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   277 AA;  29187 MW;  2DEE6DFEB9080AE0 CRC64;
     MAAYMEHKDL ANESIGPERT RQITDGVHRV LDRIASAERA AGREAGSVRL LAATKTRDVG
     EIVAAIDAGV RMIGENRPQE VVAKVEGLRR LCRERGYALG ADGGDAADGG ASAVAGHIPF
     HLIGQLQSNK INKVLPVVDT IESVDSVELA EKIARRAVAA GITVGVLLEV NESGEASKSG
     CDPALALDIA RRIGAMGGVE LQGLMTIGAH VDDERVIRAG FAHLRRLREQ ILASGDPGTG
     HCLELSMGMT QDMELAIAEG STIVRVGTAI FGERAFK
//
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