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Database: UniProt
Entry: A0A0A7I4P2_9BIFI
LinkDB: A0A0A7I4P2_9BIFI
Original site: A0A0A7I4P2_9BIFI 
ID   A0A0A7I4P2_9BIFI        Unreviewed;       280 AA.
AC   A0A0A7I4P2;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=AH68_09150 {ECO:0000313|EMBL:AIZ15173.1};
OS   Bifidobacterium catenulatum PV20-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ15173.1, ECO:0000313|Proteomes:UP000030625};
RN   [1] {ECO:0000313|EMBL:AIZ15173.1, ECO:0000313|Proteomes:UP000030625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ15173.1,
RC   ECO:0000313|Proteomes:UP000030625};
RX   PubMed=25614572;
RA   Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA   Stevens M.J.;
RT   "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT   PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL   Genome Announc. 3:0-0(2015).
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; CP007456; AIZ15173.1; -; Genomic_DNA.
DR   RefSeq; WP_039199311.1; NZ_CP007456.1.
DR   AlphaFoldDB; A0A0A7I4P2; -.
DR   STRING; 1447716.AH68_09150; -.
DR   KEGG; bka:AH68_09150; -.
DR   HOGENOM; CLU_059988_1_0_11; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000030625; 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}.
FT   DOMAIN          47..277
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   280 AA;  29714 MW;  D1133E81E56B5CB2 CRC64;
     MTAYMDHKNL ANEVIDDVRA VQIADGVHRV LDRIASAEQH AGRDAGSVRL LAATKTRDVG
     EIMAAIDAGV RMIGENRPQE VTAKAEGLMA RCAERGFALG VAGDSGIASA SDDSEVACER
     IPFHLIGQLQ SNKIGKVLPV VNAIESVDSL DLAEKISRRA VARGVTVGVL LEVNESGEAS
     KSGCNPAYAI RVAQKIGTLD GLELQGLMTI GAHVSDETAI RRGFEHLRRT RDHILESGEP
     GTQSCRELSM GMTGDMELAI AEGSTIVRVG TAIFGERAFI
//
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