ID E0RV75_BUTPB Unreviewed; 230 AA.
AC E0RV75;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=bpr_I1758 {ECO:0000313|EMBL:ADL34494.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL34494.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL34494.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
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; CP001810; ADL34494.1; -; Genomic_DNA.
DR RefSeq; WP_013281148.1; NC_014387.1.
DR AlphaFoldDB; E0RV75; -.
DR STRING; 515622.bpr_I1758; -.
DR KEGG; bpb:bpr_I1758; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_1_0_9; -.
DR Proteomes; UP000001299; Chromosome 1.
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.
DR PROSITE; PS01211; UPF0001; 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:UP000001299}.
FT DOMAIN 5..226
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 34
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 230 AA; 25612 MW; C6454153AA5DDB33 CRC64;
MIKENLEMVE ANIQSACKRA GRDRSEVTLI AVSKTKPVSD IREAMACGIK VFGENKVQEI
RDKTAEITEP LSWHMIGHLQ ANKVKYLPGV ACMIHSVDNV KLADEIEKQA AKHDIVMDVL
VEVNMAHEDT KFGISPDEAA DFVKEISVNK HINIRGLMTI APYTENPESN RVYFKGLREL
KDKINAMNIS GVHMDTLSMG MTGDYEVAIE EGATFVRVGT GIFGERNYSK
//
