ID   A0A151BYV8_9MICO        Unreviewed;       282 AA.
AC   A0A151BYV8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Pyridoxal kinase {ECO:0000313|EMBL:KYH45169.1};
GN   ORFNames=AZH51_14920 {ECO:0000313|EMBL:KYH45169.1};
OS   Branchiibius sp. NY16-3462-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Branchiibius.
OX   NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH45169.1, ECO:0000313|Proteomes:UP000075667};
RN   [1] {ECO:0000313|EMBL:KYH45169.1, ECO:0000313|Proteomes:UP000075667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH45169.1};
RA   Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT   "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT   sample.";
RL   Submitted (MAR-2016) 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:KYH45169.1}.
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DR   EMBL; LVCF01000025; KYH45169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BYV8; -.
DR   STRING; 1807500.AZH51_14920; -.
DR   Proteomes; UP000075667; 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   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:KYH45169.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075667};
KW   Transferase {ECO:0000313|EMBL:KYH45169.1}.
FT   DOMAIN          73..250
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   282 AA;  29803 MW;  4EBFE1BA68CD5859 CRC64;
     MKVLSIQSSV AYGHAGNSSA VFPLQRLGHE VWPVYTVHFS NHTGYGQWRG PVFSPETVAD
     VVLGIEERGV LPQCDAVLSG YMGDAEIGEV ILDAVARVKA ANPAAVYCAD PVMGDVGRGF
     FVREGIPEFM RDRVVPVADI LTPNQFELEY LTGGPIATVD ELLTAVDGVR ARGPKTVLVT
     SVQTDETPAD SVQMVLATDA GAWLVTTPLL PMYVSGAGDA TAAIFLAHVL SQDPATALAE
     TADSVFTIMA TTHEAGSREI ALIAAQDGIA HPSGQFEAVR LR
//