ID A0A7K5XWC7_9CHAR Unreviewed; 285 AA.
AC A0A7K5XWC7;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Pyridoxal kinase {ECO:0000256|ARBA:ARBA00018134};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
DE AltName: Full=Pyridoxine kinase {ECO:0000256|ARBA:ARBA00032808};
DE Flags: Fragment;
GN Name=Pdxk {ECO:0000313|EMBL:NWU57370.1};
GN ORFNames=DROARD_R10635 {ECO:0000313|EMBL:NWU57370.1};
OS Dromas ardeola.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Dromadidae;
OC Dromas.
OX NCBI_TaxID=458190 {ECO:0000313|EMBL:NWU57370.1, ECO:0000313|Proteomes:UP000586671};
RN [1] {ECO:0000313|EMBL:NWU57370.1, ECO:0000313|Proteomes:UP000586671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-012-55 {ECO:0000313|EMBL:NWU57370.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWU57370.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6
CC vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form
CC pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and
CC pyridoxamine 5'-phosphate (PMP), respectively. PLP is the active form
CC of vitamin B6, and acts as a cofactor for over 140 different enzymatic
CC reactions. {ECO:0000256|ARBA:ARBA00045787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyridoxal + ATP = pyridoxal 5'-phosphate + ADP + H(+);
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|ARBA:ARBA00047377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC Evidence={ECO:0000256|ARBA:ARBA00047377};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyridoxamine + ATP = pyridoxamine 5'-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216;
CC EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00047310};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105;
CC Evidence={ECO:0000256|ARBA:ARBA00047310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pyridoxine + ATP = pyridoxine 5'-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216;
CC EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00048524};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109;
CC Evidence={ECO:0000256|ARBA:ARBA00048524};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000256|ARBA:ARBA00005210}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004750}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC pyridoxine 5'-phosphate from pyridoxine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004835}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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:NWU57370.1}.
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DR EMBL; VYZM01019490; NWU57370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K5XWC7; -.
DR UniPathway; UPA01068; UER00298.
DR Proteomes; UP000586671; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR FunFam; 3.40.1190.20:FF:000007; Pyridoxal 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:NWU57370.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000586671};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 67..254
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWU57370.1"
FT NON_TER 285
FT /evidence="ECO:0000313|EMBL:NWU57370.1"
SQ SEQUENCE 285 AA; 31721 MW; 89F8616B20C43D72 CRC64;
LQVLGFEVDT VNSVQFSNHT GYAHWKGQVL NSDELHELYE GLKLNKVNQY DYVLTGYTRD
TSFLAMVVDI VQELKQQNSN LVYVCDPVMG DKWNGEGSMY VPKDLLPVYR DKVVPVADII
TPNQFEAELL TGRKIQTEKE ALEVMDMLHA MGPETVVITS SDLQAPLGND YLIALGSHRK
TKADGTKVTQ RIRVESPKVD AVFVGTGDLF AAMLLAWTHK HPNNLKVACE KTVSAMQHVL
QRTIKSAKAQ AGEGNKPNSA QLELRMVQSK KDIENPEIIV KATVL
//
