ID A0A0B8P425_9VIBR Unreviewed; 206 AA.
AC A0A0B8P425;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=JCM19231_343 {ECO:0000313|EMBL:GAM58043.1};
OS Vibrio ishigakensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM58043.1, ECO:0000313|Proteomes:UP000031671};
RN [1] {ECO:0000313|EMBL:GAM58043.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAM58043.1, ECO:0000313|Proteomes:UP000031671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG NBRP consortium;
RA Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL Submitted (JAN-2015) 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:GAM58043.1}.
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DR EMBL; BBRZ01000072; GAM58043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B8P425; -.
DR Proteomes; UP000031671; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031671}.
FT DOMAIN 3..202
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 8
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 206 AA; 23187 MW; 7FE15064A03C608E CRC64;
MQLLAVSKTK PNQAILDAIE AGHRQFGENY VQEGVEKIQY FQEHHSQFDI EWHFIGPIQS
NKTKPIAENF DWVHSVERAK IAKRLSDQRG EDKEPLQVLI QVNTSAEESK SGVHEQEALE
LAKTISELPN ITLRGLMSIP ANVQDYQQQL DAFNELKALF EQLKAQYPQV DTLSMGMSGD
MQAAVEAGSS MVRIGTAIFG ARDYKK
//
