PDXY_VIBC1
ID PDXY_VIBC1 Reviewed; 289 AA.
AC A7N5Q6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Pyridoxal kinase PdxY {ECO:0000255|HAMAP-Rule:MF_01639};
DE Short=PL kinase {ECO:0000255|HAMAP-Rule:MF_01639};
DE EC=2.7.1.35 {ECO:0000255|HAMAP-Rule:MF_01639};
GN Name=pdxY {ECO:0000255|HAMAP-Rule:MF_01639};
GN OrderedLocusNames=VIBHAR_04836;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal
CC 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
CC {ECO:0000255|HAMAP-Rule:MF_01639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC EC=2.7.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01639};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01639};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01639}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01639}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01639}.
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DR EMBL; CP000790; ABU72745.1; -; Genomic_DNA.
DR RefSeq; WP_011999144.1; NC_022270.1.
DR AlphaFoldDB; A7N5Q6; -.
DR SMR; A7N5Q6; -.
DR EnsemblBacteria; ABU72745; ABU72745; VIBHAR_04836.
DR KEGG; vha:VIBHAR_04836; -.
DR PATRIC; fig|338187.25.peg.5352; -.
DR OMA; CPNQLEL; -.
DR OrthoDB; 1480223at2; -.
DR UniPathway; UPA01068; UER00298.
DR Proteomes; UP000008152; Chromosome II.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:UniProtKB-UniRule.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01639; PdxY; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR023685; Pyridoxal_kinase_PdxY.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR10534; PTHR10534; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Nucleotide-binding; Transferase.
FT CHAIN 1..289
FT /note="Pyridoxal kinase PdxY"
FT /id="PRO_1000069890"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ SEQUENCE 289 AA; 31406 MW; 4476EB0FE24FF684 CRC64;
MQGILSIQSH VSFGHAGNSS AVFPMQRMGF EVWPIHTVQF SNHTQHQEGW TGRAFSADDI
SELVRGLGNI GALEKCQAVL TGYQGSAEQC LAVEDTVTKV KQANPEALYV CDPVMGAPDK
GCIVAPGIAE NLLNRLMPMA DVIVPNQFEL SQFAEMEIHT LDDAINACQR ALAKGPKVVL
VKHLYCLSDD SFNMLLATSE GTYLAKRPHF EFAKAPVGAG DLISAIFTAG LLKGWTPKQA
FQHCHDACYG VLNATYQAGE WELQTIAAQQ EFVEPSAHFP LEEVTLSQA
