ID A0A7K4U014_9SYLV Unreviewed; 320 AA.
AC A0A7K4U014;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
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:NWR03525.1};
GN ORFNames=SINWEB_R07113 {ECO:0000313|EMBL:NWR03525.1};
OS Sinosuthora webbiana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Sinosuthora.
OX NCBI_TaxID=337173 {ECO:0000313|EMBL:NWR03525.1, ECO:0000313|Proteomes:UP000580691};
RN [1] {ECO:0000313|EMBL:NWR03525.1, ECO:0000313|Proteomes:UP000580691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-08 {ECO:0000313|EMBL:NWR03525.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWR03525.1};
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:NWR03525.1}.
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DR EMBL; VXBN01006331; NWR03525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K4U014; -.
DR OrthoDB; 2104723at2759; -.
DR UniPathway; UPA01068; UER00298.
DR Proteomes; UP000580691; 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:NWR03525.1};
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:UP000580691};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 102..292
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWR03525.1"
FT NON_TER 320
FT /evidence="ECO:0000313|EMBL:NWR03525.1"
SQ SEQUENCE 320 AA; 35542 MW; F9C44B2E21179021 CRC64;
RAGARGAAME PECRVLSIQS HVVRGYVGNK AATFPLQVLG FEVDTVNSVQ FSNHTGYAHW
KGQVLNSDEL HELYEGLKLN KVNRYDYVLT GYTRDTSFLA MVVDIVQELK QQNPNLVYVC
DPVMGDKWNG EGSMYVPKDL LPVYRDKVVP VADIITPNQF EAELLTGRKI YTEKDALEVM
DMLHAMGPET VVITSSDLQA PLGNDYLIAL GSHRKTKADG TRITQRIRVE SPKVDAVFVG
TGDLFAAMLL AWTHKHPNNL KVACEKTVSA MQHVLQRTIK SAKVQAGEGN KPNSAHLELR
MVQSKKDIEN PEIIVKATVL
//
