ID G8PV44_PSEUV Unreviewed; 294 AA.
AC G8PV44;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN Name=pdxY {ECO:0000313|EMBL:AEV39632.1};
GN OrderedLocusNames=PSE_p0050 {ECO:0000313|EMBL:AEV39632.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OG Plasmid FO-BEG1 {ECO:0000313|Proteomes:UP000005634}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39632.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RC PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV39632.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV39632.1,
RC ECO:0000313|Proteomes:UP000005634};
RC PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003148; AEV39632.1; -; Genomic_DNA.
DR AlphaFoldDB; G8PV44; -.
DR KEGG; psf:PSE_p0050; -.
DR eggNOG; COG2240; Bacteria.
DR HOGENOM; CLU_046496_3_0_5; -.
DR Proteomes; UP000005634; Plasmid FO-BEG1.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AEV39632.1};
KW Plasmid {ECO:0000313|EMBL:AEV39632.1};
KW Transferase {ECO:0000313|EMBL:AEV39632.1}.
FT DOMAIN 91..270
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 294 AA; 32165 MW; FD4C5F8C623B5CDF CRC64;
MSLSLNEEIE MKGILSIQSH VTYGHAGNGC AVFPMQRMGH EVWAINTVQF SNHTQHPQGW
TGQAHDAKQI SEIFEGLAKL NVLSQIKGIV TGYLGGPSHC DVIVDIVQEV RRHNPDCLYF
CDPVMGAPDK GCIVSEGVAE LLVSKVMPIA DVIVPNQFEL SQFIGEPVET LEQAKQACAK
AMEKGPKMVL AKHLHSVSDE AFTMTFANAQ GSYLAQRPHL PFERQPVGVG DLITSVFAAG
YLNGLSEVEA FQHCNNAVYG VLKTTQEKGE WELQTIAAQQ EFVSPSEQFD LISL
//
