ID   A0A0B2AXX8_9ACTN        Unreviewed;       285 AA.
AC   A0A0B2AXX8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Pyridoxine kinase {ECO:0000313|EMBL:PJJ56048.1};
GN   ORFNames=CLV56_0252 {ECO:0000313|EMBL:PJJ56048.1};
OS   Mumia flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Mumia.
OX   NCBI_TaxID=1348852 {ECO:0000313|EMBL:PJJ56048.1, ECO:0000313|Proteomes:UP000230842};
RN   [1] {ECO:0000313|EMBL:PJJ56048.1, ECO:0000313|Proteomes:UP000230842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27763 {ECO:0000313|EMBL:PJJ56048.1,
RC   ECO:0000313|Proteomes:UP000230842};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) 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:PJJ56048.1}.
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DR   EMBL; PGEZ01000001; PJJ56048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2AXX8; -.
DR   OrthoDB; 9800808at2; -.
DR   Proteomes; UP000230842; 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:PJJ56048.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230842};
KW   Transferase {ECO:0000313|EMBL:PJJ56048.1}.
FT   DOMAIN          74..242
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   285 AA;  29830 MW;  D07C7AE64A4F8459 CRC64;
     MQVLSIQSQV AYGHAGNSSA VFPLQRLGVD VWPVNTVGFS NHSGYGVWRG TVYEASQVAD
     VVTGVAERGV LPGIDAVLSG YQGSPDIGEV ILDAVEQVKA ANPRAVYCAD PVIGDRGRGV
     YVRPGIAELM RDRIVPAADL TTPNQFELEL LAGGPVGTLD ELLDAVAALR ARGPRTVLVT
     SVEVLDPGGD TISMVGVDPS GAYVVTTPML TMKVVAGSGD ATTAMFLGRM LQSGMDLPGS
     LERVASSIFG VLDHTRRTDA AEMELVAAQD VIANPPTEFA VERLV
//