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
//