ID B8KLD9_9GAMM Unreviewed; 230 AA.
AC B8KLD9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=NOR53_2955 {ECO:0000313|EMBL:EED31906.1};
OS gamma proteobacterium NOR5-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=566466 {ECO:0000313|EMBL:EED31906.1};
RN [1] {ECO:0000313|EMBL:EED31906.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NOR5-3 {ECO:0000313|EMBL:EED31906.1};
RA Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (SEP-2008) 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; DS999406; EED31906.1; -; Genomic_DNA.
DR AlphaFoldDB; B8KLD9; -.
DR STRING; 566466.NOR53_2955; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_0_1_6; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000003977; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR CDD; cd06824; PLPDE_III_Yggs_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}.
FT DOMAIN 26..228
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 38
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 230 AA; 24878 MW; 4E41AE74E4294E38 CRC64;
MNNDSIPANI AKVLQQVSNA VEKYHRPPQS VRVMAVSKTQ SAEAVRTAAN AGLTDFGENY
LQEALDKIAA CEDLGLTWHF IGPIQSNKTR PIATSFHWVH SVDREKILRR LSEQRDANLP
ALNICIQVNV SREASKSGVA PEDLPPLLAL TAGLPNLELR GLMAIPAASD DFATQKQACD
LMATLFHEAQ SQYPSLDTLS MGMSADLEAA VAAGSNMLRI GTAIFGARQR
//
