ID A0A1G7SR82_9ACTN Unreviewed; 283 AA.
AC A0A1G7SR82;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pyridoxal kinase PdxY {ECO:0000256|HAMAP-Rule:MF_01639};
DE Short=PL kinase {ECO:0000256|HAMAP-Rule:MF_01639};
DE EC=2.7.1.35 {ECO:0000256|HAMAP-Rule:MF_01639};
GN Name=pdxY {ECO:0000256|HAMAP-Rule:MF_01639};
GN ORFNames=SAMN05660324_2133 {ECO:0000313|EMBL:SDG25565.1};
OS Klenkia brasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=333142 {ECO:0000313|EMBL:SDG25565.1, ECO:0000313|Proteomes:UP000198863};
RN [1] {ECO:0000313|EMBL:SDG25565.1, ECO:0000313|Proteomes:UP000198863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44526 {ECO:0000313|EMBL:SDG25565.1,
RC ECO:0000313|Proteomes:UP000198863};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|HAMAP-Rule:MF_01639}.
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 -!- 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:0000256|HAMAP-Rule:MF_01639};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01639};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01639}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01639}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01639}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01639}.
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DR EMBL; FNCF01000003; SDG25565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7SR82; -.
DR OrthoDB; 9800808at2; -.
DR UniPathway; UPA01068; UER00298.
DR Proteomes; UP000198863; Unassembled WGS sequence.
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 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01639};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01639, ECO:0000313|EMBL:SDG25565.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01639};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01639};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01639}.
FT DOMAIN 74..258
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01639"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01639"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01639"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01639"
SQ SEQUENCE 283 AA; 29240 MW; DFF9655C0FB89208 CRC64;
MAVVLSIQSH VAYGHVGNAS AVFPLQRLGH EVWPVHTVQF SNHTGYGSWT GRVFDGQAVE
EVVDGIAARG VLGSCDAVLS GYLGSADIGH AVVGTVARVR EANPAAVYCC DPVIGDVGRG
VFVRPGIAEF MRDVAVPAAD VVTPNHFELD LLTGGTTTTL PQVRDAVAAL QATGPQVVLV
TSLDVEDTPD DAVDLLAAAG GRAWRVRTPE LGLSVNGAGD AIAALFLAHW MSTGSAADAL
GAAAASVFGL LRMTAEAGSR EILTVAAQEE FVSPTRTFEV VEV
//