ID A0A087B3V1_9BIFI Unreviewed; 289 AA.
AC A0A087B3V1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Pyridoxine kinase {ECO:0000313|EMBL:KFI65701.1};
DE EC=2.7.1.35 {ECO:0000313|EMBL:KFI65701.1};
GN ORFNames=BCUN_0196 {ECO:0000313|EMBL:KFI65701.1};
OS Bifidobacterium cuniculi.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65701.1, ECO:0000313|Proteomes:UP000029067};
RN [1] {ECO:0000313|EMBL:KFI65701.1, ECO:0000313|Proteomes:UP000029067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65701.1,
RC ECO:0000313|Proteomes:UP000029067};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000565};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
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:KFI65701.1}.
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DR EMBL; JGYV01000001; KFI65701.1; -; Genomic_DNA.
DR RefSeq; WP_033515041.1; NZ_JGYV01000001.1.
DR AlphaFoldDB; A0A087B3V1; -.
DR STRING; 1688.BCUN_0196; -.
DR eggNOG; COG2240; Bacteria.
DR OrthoDB; 9800808at2; -.
DR Proteomes; UP000029067; Unassembled WGS sequence.
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 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:KFI65701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW Transferase {ECO:0000313|EMBL:KFI65701.1}.
FT DOMAIN 38..262
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 289 AA; 30751 MW; A33B4A2021BBE3F1 CRC64;
MSTVLYERNR TYIPRIAAVH DMCGYGKCSL TAAIPILSAA GCDVLPVPTA LFSAHTKFPV
FTMTDTTDML SGYLDAWQQE GVELDGVYSG FLGAPEQVAI IQRLYEEHPG ALRLVDPVMG
DGGQMYATYT QELCDAMGAL ADGADILMPN LTEASILTGT EYLGNDLSDA QVDALLQALL
DLGARNVVLK GIDHGDGRIR NFVAGADEGV GAKVELVHEK LPYMCHGTGD AFASALIGGV
MAGLDLPGAA RLAGEFVRNA MISTKHQPDY EMRGVSFELC LGELADLVD
//
