PDXK_SHEEP
ID PDXK_SHEEP Reviewed; 312 AA.
AC P82197; Q9XSD8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35 {ECO:0000250|UniProtKB:O00764};
DE AltName: Full=Pyridoxine kinase;
GN Name=PDXK; Synonyms=PKH;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE OF 113-259, AND ACETYLATION AT MET-1.
RC TISSUE=Brain;
RX PubMed=10395444; DOI=10.1023/a:1021079110358;
RA Maras B., Valiante S., Orru S., Simmaco M., Barra D., Churchich J.E.;
RT "Structure of pyridoxal kinase from sheep brain and role of the
RT tryptophanyl residues.";
RL J. Protein Chem. 18:259-268(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-312.
RC TISSUE=Liver;
RA Kwon O.-S., Lee H.-S.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=12198308; DOI=10.1107/s0907444902011034;
RA Li M.-H., Kwok F., An X.-M., Chang W.-R., Lau C.-K., Zhang J.-P.,
RA Liu S.-Q., Leung Y.-C., Jiang T., Liang D.-C.;
RT "Crystallization and preliminary crystallographic studies of pyridoxal
RT kinase from sheep brain.";
RL Acta Crystallogr. D 58:1479-1481(2002).
RN [4] {ECO:0007744|PDB:1LHP, ECO:0007744|PDB:1LHR}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP ZN-ATP AND POTASSIUM, AND COFACTOR.
RX PubMed=12235162; DOI=10.1074/jbc.m208600200;
RA Li M.H., Kwok F., Chang W.R., Lau C.K., Zhang J.P., Lo S.C., Jiang T.,
RA Liang D.C.;
RT "Crystal structure of brain pyridoxal kinase, a novel member of the
RT ribokinase superfamily.";
RL J. Biol. Chem. 277:46385-46390(2002).
RN [5] {ECO:0007744|PDB:1RFT, ECO:0007744|PDB:1RFU, ECO:0007744|PDB:1RFV}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEXES WITH ADP; ATP ANALOG;
RP POTASSIUM; PYRIDOXAL PHOSPHATE AND PYRIDOXAMINE, FUNCTION, AND COFACTOR.
RX PubMed=14722069; DOI=10.1074/jbc.m312380200;
RA Li M.H., Kwok F., Chang W.R., Liu S.Q., Lo S.C., Zhang J.P., Jiang T.,
RA Liang D.C.;
RT "Conformational changes in the reaction of pyridoxal kinase.";
RL J. Biol. Chem. 279:17459-17465(2004).
RN [6] {ECO:0007744|PDB:1YGJ, ECO:0007744|PDB:1YGK, ECO:0007744|PDB:1YHJ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEXES WITH ROSCOVITINE AND
RP DERIVATIVES.
RX PubMed=15985434; DOI=10.1074/jbc.m500805200;
RA Tang L., Li M.H., Cao P., Wang F., Chang W.R., Bach S., Reinhardt J.,
RA Ferandin Y., Galons H., Wan Y., Gray N., Meijer L., Jiang T., Liang D.C.;
RT "Crystal structure of pyridoxal kinase in complex with roscovitine and
RT derivatives.";
RL J. Biol. Chem. 280:31220-31229(2005).
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 (PubMed:14722069) (By
CC similarity). PLP is the active form of vitamin B6, and acts as a
CC cofactor for over 140 different enzymatic reactions (By similarity).
CC {ECO:0000250|UniProtKB:O00764, ECO:0000305|PubMed:14722069}.
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:0000250|UniProtKB:O00764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate;
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:0000250|UniProtKB:O00764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate;
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:0000250|UniProtKB:O00764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:12235162, ECO:0000305|PubMed:14722069};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- ACTIVITY REGULATION: Activated by K(+) (Probable). Activity is
CC increased in the presence of Na(+) (By similarity).
CC {ECO:0000250|UniProtKB:O00764, ECO:0000305|PubMed:12235162,
CC ECO:0000305|PubMed:14722069}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000250|UniProtKB:O00764}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC pyridoxine 5'-phosphate from pyridoxine: step 1/1.
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12198308,
CC ECO:0000269|PubMed:12235162, ECO:0000269|PubMed:14722069}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
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DR EMBL; AF125374; AAD34353.1; -; mRNA.
DR RefSeq; NP_001009220.1; NM_001009220.1.
DR PDB; 1LHP; X-ray; 2.10 A; A/B=1-312.
DR PDB; 1LHR; X-ray; 2.60 A; A/B=1-312.
DR PDB; 1RFT; X-ray; 2.80 A; A=1-312.
DR PDB; 1RFU; X-ray; 2.80 A; A/B/C/D/E/F/G/H=1-312.
DR PDB; 1RFV; X-ray; 2.80 A; A/B=1-312.
DR PDB; 1YGJ; X-ray; 2.70 A; A=1-312.
DR PDB; 1YGK; X-ray; 2.60 A; A=1-312.
DR PDB; 1YHJ; X-ray; 2.80 A; A=1-312.
DR PDBsum; 1LHP; -.
DR PDBsum; 1LHR; -.
DR PDBsum; 1RFT; -.
DR PDBsum; 1RFU; -.
DR PDBsum; 1RFV; -.
DR PDBsum; 1YGJ; -.
DR PDBsum; 1YGK; -.
DR PDBsum; 1YHJ; -.
DR AlphaFoldDB; P82197; -.
DR SMR; P82197; -.
DR STRING; 9940.ENSOARP00000012160; -.
DR iPTMnet; P82197; -.
DR GeneID; 443049; -.
DR KEGG; oas:443049; -.
DR CTD; 8566; -.
DR eggNOG; KOG2599; Eukaryota.
DR OrthoDB; 1091630at2759; -.
DR BRENDA; 2.7.1.35; 2668.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR EvolutionaryTrace; P82197; -.
DR Proteomes; UP000002356; Unplaced.
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: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 PANTHER; PTHR10534; PTHR10534; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Potassium; Reference proteome; Sodium;
KW Transferase.
FT CHAIN 1..312
FT /note="Pyridoxal kinase"
FT /id="PRO_0000213339"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 12
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU"
FT BINDING 12
FT /ligand="pyridoxamine"
FT /ligand_id="ChEBI:CHEBI:57761"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFT"
FT BINDING 47
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU"
FT BINDING 47
FT /ligand="pyridoxamine"
FT /ligand_id="ChEBI:CHEBI:57761"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFT"
FT BINDING 113
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR,
FT ECO:0007744|PDB:1RFT"
FT BINDING 127
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU"
FT BINDING 148
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR,
FT ECO:0007744|PDB:1RFT"
FT BINDING 150
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1RFU,
FT ECO:0007744|PDB:1RFV"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR"
FT BINDING 186..187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU, ECO:0007744|PDB:1RFV"
FT BINDING 186..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0007744|PDB:1LHR"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0000269|PubMed:14722069, ECO:0007744|PDB:1LHR,
FT ECO:0007744|PDB:1RFT"
FT BINDING 223..226
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU, ECO:0007744|PDB:1RFV"
FT BINDING 223..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0007744|PDB:1LHR"
FT BINDING 232..235
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU"
FT BINDING 233..234
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFU, ECO:0007744|PDB:1RFV"
FT BINDING 233..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12235162,
FT ECO:0007744|PDB:1LHR"
FT BINDING 235
FT /ligand="pyridoxamine"
FT /ligand_id="ChEBI:CHEBI:57761"
FT /evidence="ECO:0000269|PubMed:14722069,
FT ECO:0007744|PDB:1RFT"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:10395444"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT CONFLICT 16..47
FT /note="RGYVGNRAATFPLQVLGFEVDAVNSVQFSNHT -> MCFGGTAESLCPGDLM
FT QHRGLTWSALPPTPPP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="EL -> DV (in Ref. 2; AAD34353)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="N -> D (in Ref. 2; AAD34353)"
FT /evidence="ECO:0000305"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1YGJ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1YGJ"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1YGK"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 252..277
FT /evidence="ECO:0007829|PDB:1LHP"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1YGK"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1LHP"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:1LHP"
SQ SEQUENCE 312 AA; 34819 MW; C5F286DBCF51CA6A CRC64;
MEEECRVLSI QSHVVRGYVG NRAATFPLQV LGFEVDAVNS VQFSNHTGYS HWKGQVLNSD
ELQELYDGLK LNHVNQYDYV LTGYTRDKSF LAMVVDIVQE LKQQNPRLVY VCDPVMGDQR
NGEGAMYVPD DLLPVYREKV VPVADIITPN QFEAELLTGR KIHSQEEALE VMDMLHSMGP
DTVVITSSNL LSPRGSDYLM ALGSQRTRAP DGSVVTQRIR MEMHKVDAVF VGTGDLFAAM
LLAWTHKHPN NLKVACEKTV SAMHHVLQRT IKCAKAKSGE GVKPSPAQLE LRMVQSKKDI
ESPEIVVQAT VL
