Full text data of PDXK
PDXK
(C21orf124, C21orf97, PKH, PNK)
[Confidence: low (only semi-automatic identification from reviews)]
Pyridoxal kinase; 2.7.1.35 (Pyridoxine kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Pyridoxal kinase; 2.7.1.35 (Pyridoxine kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00764
ID PDXK_HUMAN Reviewed; 312 AA.
AC O00764; Q7Z2Y0; Q9BS02;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35;
DE AltName: Full=Pyridoxine kinase;
GN Name=PDXK; Synonyms=C21orf124, C21orf97, PKH, PNK; ORFNames=PRED79;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9099727; DOI=10.1074/jbc.272.16.10756;
RA Hanna M.C., Turner A.J., Kirkness E.F.;
RT "Human pyridoxal kinase. cDNA cloning, expression, and modulation by
RT ligands of the benzodiazepine receptor.";
RL J. Biol. Chem. 272:10756-10760(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=15154080;
RA Fang X., Zhou Z.M., Lu L., Yin L.L., Li J.M., Zhen Y., Wang H.,
RA Sha J.H.;
RT "Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in
RT human testis.";
RL Asian J. Androl. 6:83-91(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10987144;
RA Lee H.-S., Moon B.J., Choi S.Y., Kwon O.-S.;
RT "Human pyridoxal kinase: overexpression and properties of the
RT recombinant enzyme.";
RL Mol. Cells 10:452-459(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-285, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-164; SER-213 AND
RP SER-285, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from
CC vitamin B6.
CC -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC phosphate.
CC -!- COFACTOR: Divalent cations. Zinc is more efficient than magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.0;
CC -!- SUBUNIT: Homodimer (Probable).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00764-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00764-2; Sequence=VSP_004653;
CC Note=No experimental confirmation available;
CC Name=3; Synonyms=PKH-T;
CC IsoId=O00764-3; Sequence=VSP_010671;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 3 is detected in adult
CC testis and spermatozoa.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U89606; AAC51233.1; -; mRNA.
DR EMBL; AY303972; AAP73047.1; -; mRNA.
DR EMBL; AP001752; BAA95540.1; -; Genomic_DNA.
DR EMBL; BC000123; AAH00123.1; -; mRNA.
DR EMBL; BC005825; AAH05825.1; -; mRNA.
DR RefSeq; NP_003672.1; NM_003681.4.
DR RefSeq; XP_005261254.1; XM_005261197.1.
DR RefSeq; XP_005261256.1; XM_005261199.1.
DR RefSeq; XP_005261257.1; XM_005261200.1.
DR UniGene; Hs.284491; -.
DR PDB; 2AJP; X-ray; 2.50 A; A/B=6-312.
DR PDB; 2F7K; X-ray; 2.80 A; A/B=1-312.
DR PDB; 2YXT; X-ray; 2.00 A; A/B=1-312.
DR PDB; 2YXU; X-ray; 2.20 A; A/B=1-312.
DR PDB; 3FHX; X-ray; 2.50 A; A/B=1-312.
DR PDB; 3FHY; X-ray; 2.30 A; A/B=1-312.
DR PDB; 3KEU; X-ray; 2.10 A; A/B=1-312.
DR PDB; 4EN4; X-ray; 2.15 A; A/B=1-312.
DR PDB; 4EOH; X-ray; 2.10 A; A/B=1-312.
DR PDBsum; 2AJP; -.
DR PDBsum; 2F7K; -.
DR PDBsum; 2YXT; -.
DR PDBsum; 2YXU; -.
DR PDBsum; 3FHX; -.
DR PDBsum; 3FHY; -.
DR PDBsum; 3KEU; -.
DR PDBsum; 4EN4; -.
DR PDBsum; 4EOH; -.
DR ProteinModelPortal; O00764; -.
DR SMR; O00764; 3-312.
DR IntAct; O00764; 5.
DR MINT; MINT-5002166; -.
DR STRING; 9606.ENSP00000291565; -.
DR ChEMBL; CHEMBL1075181; -.
DR DrugBank; DB00147; Pyridoxal.
DR DrugBank; DB00165; Pyridoxine.
DR PhosphoSite; O00764; -.
DR REPRODUCTION-2DPAGE; IPI00013004; -.
DR REPRODUCTION-2DPAGE; O00764; -.
DR PaxDb; O00764; -.
DR PRIDE; O00764; -.
DR DNASU; 8566; -.
DR Ensembl; ENST00000291565; ENSP00000291565; ENSG00000160209.
DR Ensembl; ENST00000468090; ENSP00000418359; ENSG00000160209.
DR GeneID; 8566; -.
DR KEGG; hsa:8566; -.
DR UCSC; uc002zdm.4; human.
DR CTD; 8566; -.
DR GeneCards; GC21P045138; -.
DR HGNC; HGNC:8819; PDXK.
DR HPA; CAB033918; -.
DR HPA; HPA030196; -.
DR HPA; HPA030197; -.
DR HPA; HPA030198; -.
DR MIM; 179020; gene.
DR neXtProt; NX_O00764; -.
DR PharmGKB; PA33162; -.
DR eggNOG; COG2240; -.
DR HOGENOM; HOG000258174; -.
DR HOVERGEN; HBG000732; -.
DR InParanoid; O00764; -.
DR KO; K00868; -.
DR OMA; RIRMEMH; -.
DR PhylomeDB; O00764; -.
DR BRENDA; 2.7.1.35; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; O00764; -.
DR ChiTaRS; PDXK; human.
DR EvolutionaryTrace; O00764; -.
DR GeneWiki; PDXK; -.
DR GenomeRNAi; 8566; -.
DR NextBio; 32117; -.
DR PRO; PR:O00764; -.
DR ArrayExpress; O00764; -.
DR Bgee; O00764; -.
DR CleanEx; HS_PDXK; -.
DR Genevestigator; O00764; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0031403; F:lithium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008478; F:pyridoxal kinase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042816; P:vitamin B6 metabolic process; IC:UniProtKB.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR PANTHER; PTHR10534; PTHR10534; 1.
DR Pfam; PF00294; PfkB; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Zinc.
FT CHAIN 1 312 Pyridoxal kinase.
FT /FTId=PRO_0000213335.
FT NP_BIND 186 187 ATP (By similarity).
FT NP_BIND 223 234 ATP (By similarity).
FT BINDING 12 12 Substrate (By similarity).
FT BINDING 47 47 Substrate (By similarity).
FT BINDING 127 127 Substrate (By similarity).
FT BINDING 235 235 Substrate (By similarity).
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 59 59 Phosphoserine.
FT MOD_RES 164 164 Phosphoserine.
FT MOD_RES 213 213 Phosphoserine.
FT MOD_RES 285 285 Phosphoserine.
FT VAR_SEQ 1 73 Missing (in isoform 3).
FT /FTId=VSP_010671.
FT VAR_SEQ 83 110 Missing (in isoform 2).
FT /FTId=VSP_004653.
FT STRAND 6 17
FT HELIX 21 30
FT STRAND 34 45
FT STRAND 54 56
FT HELIX 59 71
FT STRAND 78 82
FT HELIX 88 104
FT STRAND 109 112
FT STRAND 117 119
FT STRAND 120 123
FT STRAND 125 128
FT HELIX 132 138
FT HELIX 141 143
FT STRAND 145 147
FT HELIX 151 158
FT HELIX 165 178
FT STRAND 181 185
FT STRAND 198 207
FT TURN 210 212
FT STRAND 215 224
FT HELIX 233 247
FT HELIX 252 277
FT TURN 286 289
FT HELIX 294 296
FT HELIX 297 301
FT STRAND 310 312
SQ SEQUENCE 312 AA; 35102 MW; 2DBDCAB5D8640569 CRC64;
MEEECRVLSI QSHVIRGYVG NRAATFPLQV LGFEIDAVNS VQFSNHTGYA HWKGQVLNSD
ELQELYEGLR LNNMNKYDYV LTGYTRDKSF LAMVVDIVQE LKQQNPRLVY VCDPVLGDKW
DGEGSMYVPE DLLPVYKEKV VPLADIITPN QFEAELLSGR KIHSQEEALR VMDMLHSMGP
DTVVITSSDL PSPQGSNYLI VLGSQRRRNP AGSVVMERIR MDIRKVDAVF VGTGDLFAAM
LLAWTHKHPN NLKVACEKTV STLHHVLQRT IQCAKAQAGE GVRPSPMQLE LRMVQSKRDI
EDPEIVVQAT VL
//
ID PDXK_HUMAN Reviewed; 312 AA.
AC O00764; Q7Z2Y0; Q9BS02;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1997, sequence version 1.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35;
DE AltName: Full=Pyridoxine kinase;
GN Name=PDXK; Synonyms=C21orf124, C21orf97, PKH, PNK; ORFNames=PRED79;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9099727; DOI=10.1074/jbc.272.16.10756;
RA Hanna M.C., Turner A.J., Kirkness E.F.;
RT "Human pyridoxal kinase. cDNA cloning, expression, and modulation by
RT ligands of the benzodiazepine receptor.";
RL J. Biol. Chem. 272:10756-10760(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=15154080;
RA Fang X., Zhou Z.M., Lu L., Yin L.L., Li J.M., Zhen Y., Wang H.,
RA Sha J.H.;
RT "Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in
RT human testis.";
RL Asian J. Androl. 6:83-91(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
RA Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10987144;
RA Lee H.-S., Moon B.J., Choi S.Y., Kwon O.-S.;
RT "Human pyridoxal kinase: overexpression and properties of the
RT recombinant enzyme.";
RL Mol. Cells 10:452-459(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-285, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-164; SER-213 AND
RP SER-285, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from
CC vitamin B6.
CC -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC phosphate.
CC -!- COFACTOR: Divalent cations. Zinc is more efficient than magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.0;
CC -!- SUBUNIT: Homodimer (Probable).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00764-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00764-2; Sequence=VSP_004653;
CC Note=No experimental confirmation available;
CC Name=3; Synonyms=PKH-T;
CC IsoId=O00764-3; Sequence=VSP_010671;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 3 is detected in adult
CC testis and spermatozoa.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U89606; AAC51233.1; -; mRNA.
DR EMBL; AY303972; AAP73047.1; -; mRNA.
DR EMBL; AP001752; BAA95540.1; -; Genomic_DNA.
DR EMBL; BC000123; AAH00123.1; -; mRNA.
DR EMBL; BC005825; AAH05825.1; -; mRNA.
DR RefSeq; NP_003672.1; NM_003681.4.
DR RefSeq; XP_005261254.1; XM_005261197.1.
DR RefSeq; XP_005261256.1; XM_005261199.1.
DR RefSeq; XP_005261257.1; XM_005261200.1.
DR UniGene; Hs.284491; -.
DR PDB; 2AJP; X-ray; 2.50 A; A/B=6-312.
DR PDB; 2F7K; X-ray; 2.80 A; A/B=1-312.
DR PDB; 2YXT; X-ray; 2.00 A; A/B=1-312.
DR PDB; 2YXU; X-ray; 2.20 A; A/B=1-312.
DR PDB; 3FHX; X-ray; 2.50 A; A/B=1-312.
DR PDB; 3FHY; X-ray; 2.30 A; A/B=1-312.
DR PDB; 3KEU; X-ray; 2.10 A; A/B=1-312.
DR PDB; 4EN4; X-ray; 2.15 A; A/B=1-312.
DR PDB; 4EOH; X-ray; 2.10 A; A/B=1-312.
DR PDBsum; 2AJP; -.
DR PDBsum; 2F7K; -.
DR PDBsum; 2YXT; -.
DR PDBsum; 2YXU; -.
DR PDBsum; 3FHX; -.
DR PDBsum; 3FHY; -.
DR PDBsum; 3KEU; -.
DR PDBsum; 4EN4; -.
DR PDBsum; 4EOH; -.
DR ProteinModelPortal; O00764; -.
DR SMR; O00764; 3-312.
DR IntAct; O00764; 5.
DR MINT; MINT-5002166; -.
DR STRING; 9606.ENSP00000291565; -.
DR ChEMBL; CHEMBL1075181; -.
DR DrugBank; DB00147; Pyridoxal.
DR DrugBank; DB00165; Pyridoxine.
DR PhosphoSite; O00764; -.
DR REPRODUCTION-2DPAGE; IPI00013004; -.
DR REPRODUCTION-2DPAGE; O00764; -.
DR PaxDb; O00764; -.
DR PRIDE; O00764; -.
DR DNASU; 8566; -.
DR Ensembl; ENST00000291565; ENSP00000291565; ENSG00000160209.
DR Ensembl; ENST00000468090; ENSP00000418359; ENSG00000160209.
DR GeneID; 8566; -.
DR KEGG; hsa:8566; -.
DR UCSC; uc002zdm.4; human.
DR CTD; 8566; -.
DR GeneCards; GC21P045138; -.
DR HGNC; HGNC:8819; PDXK.
DR HPA; CAB033918; -.
DR HPA; HPA030196; -.
DR HPA; HPA030197; -.
DR HPA; HPA030198; -.
DR MIM; 179020; gene.
DR neXtProt; NX_O00764; -.
DR PharmGKB; PA33162; -.
DR eggNOG; COG2240; -.
DR HOGENOM; HOG000258174; -.
DR HOVERGEN; HBG000732; -.
DR InParanoid; O00764; -.
DR KO; K00868; -.
DR OMA; RIRMEMH; -.
DR PhylomeDB; O00764; -.
DR BRENDA; 2.7.1.35; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR SABIO-RK; O00764; -.
DR ChiTaRS; PDXK; human.
DR EvolutionaryTrace; O00764; -.
DR GeneWiki; PDXK; -.
DR GenomeRNAi; 8566; -.
DR NextBio; 32117; -.
DR PRO; PR:O00764; -.
DR ArrayExpress; O00764; -.
DR Bgee; O00764; -.
DR CleanEx; HS_PDXK; -.
DR Genevestigator; O00764; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0031403; F:lithium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008478; F:pyridoxal kinase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042816; P:vitamin B6 metabolic process; IC:UniProtKB.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR PANTHER; PTHR10534; PTHR10534; 1.
DR Pfam; PF00294; PfkB; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Zinc.
FT CHAIN 1 312 Pyridoxal kinase.
FT /FTId=PRO_0000213335.
FT NP_BIND 186 187 ATP (By similarity).
FT NP_BIND 223 234 ATP (By similarity).
FT BINDING 12 12 Substrate (By similarity).
FT BINDING 47 47 Substrate (By similarity).
FT BINDING 127 127 Substrate (By similarity).
FT BINDING 235 235 Substrate (By similarity).
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 59 59 Phosphoserine.
FT MOD_RES 164 164 Phosphoserine.
FT MOD_RES 213 213 Phosphoserine.
FT MOD_RES 285 285 Phosphoserine.
FT VAR_SEQ 1 73 Missing (in isoform 3).
FT /FTId=VSP_010671.
FT VAR_SEQ 83 110 Missing (in isoform 2).
FT /FTId=VSP_004653.
FT STRAND 6 17
FT HELIX 21 30
FT STRAND 34 45
FT STRAND 54 56
FT HELIX 59 71
FT STRAND 78 82
FT HELIX 88 104
FT STRAND 109 112
FT STRAND 117 119
FT STRAND 120 123
FT STRAND 125 128
FT HELIX 132 138
FT HELIX 141 143
FT STRAND 145 147
FT HELIX 151 158
FT HELIX 165 178
FT STRAND 181 185
FT STRAND 198 207
FT TURN 210 212
FT STRAND 215 224
FT HELIX 233 247
FT HELIX 252 277
FT TURN 286 289
FT HELIX 294 296
FT HELIX 297 301
FT STRAND 310 312
SQ SEQUENCE 312 AA; 35102 MW; 2DBDCAB5D8640569 CRC64;
MEEECRVLSI QSHVIRGYVG NRAATFPLQV LGFEIDAVNS VQFSNHTGYA HWKGQVLNSD
ELQELYEGLR LNNMNKYDYV LTGYTRDKSF LAMVVDIVQE LKQQNPRLVY VCDPVLGDKW
DGEGSMYVPE DLLPVYKEKV VPLADIITPN QFEAELLSGR KIHSQEEALR VMDMLHSMGP
DTVVITSSDL PSPQGSNYLI VLGSQRRRNP AGSVVMERIR MDIRKVDAVF VGTGDLFAAM
LLAWTHKHPN NLKVACEKTV STLHHVLQRT IQCAKAQAGE GVRPSPMQLE LRMVQSKRDI
EDPEIVVQAT VL
//
MIM
179020
*RECORD*
*FIELD* NO
179020
*FIELD* TI
*179020 PYRIDOXAL KINASE; PDXK
;;PYRIDOXINE KINASE; PNK;;
PKH;;
VITAMIN B6 KINASE
*FIELD* TX
read more
DESCRIPTION
Pyridoxal kinase (PDXK; EC 2.7.1.35) converts vitamin B6 to
pyridoxal-5-phosphate (PLP), an essential cofactor in the intermediate
metabolism of amino acids and neurotransmitters.
CLONING
Hanna et al. (1997) cloned the cDNA encoding PDXK, which they referred
to as PKH. The PDXK gene encodes a 312-amino acid polypeptide, and
expression of the cDNA revealed pyridoxal kinase activity. Northern blot
analysis revealed that a major 1.5-kb PDXK transcript was expressed in
all tissues tested.
GENE FUNCTION
The expression of PDXK shows circadian oscillations. Gachon et al.
(2004) found that the expression of Pdxk in mouse liver and brain is
regulated by the 3 PAR bZIP transcription factors, Dbp (124097), Hlf
(142385), and Tef (179020), which also show circadian oscillations in
expression. Mice devoid of all 3 transcription factors showed decreased
levels of brain PLP, serotonin, and dopamine, and were highly
susceptible to generalized spontaneous and audiogenic epilepsies that
were frequently lethal.
MAPPING
Hanna et al. (1997) reported that a BAC clone from the human 21q22.3
region contains almost the entire PDXK gene on 10 distinct exons.
MOLECULAR GENETICS
Chern and Beutler (1976) concluded that alleles at a locus symbolized
PNK determine the level of activity of pyridoxine kinase in
erythrocytes: PNK(H) and PNK(L), for 'high' and 'low', respectively. The
frequency of these 2 alleles was estimated to be 0.81 and 0.19 for
whites and 0.35 and 0.65 for blacks. They suggested that the PNK(L)
state of red cells is the result of a stability mutation.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* RF
1. Chern, C. J.; Beutler, E.: Biochemical and electrophoretic studies
of erythrocyte pyridoxine kinase in white and black Americans. Am.
J. Hum. Genet. 28: 9-17, 1976.
2. Gachon, F.; Fonjallaz, P.; Damiola, F.; Gos, P.; Kodama, T.; Zakany,
J.; Duboule, D.; Petit, B.; Tafti, M.; Schibler, U.: The loss of
circadian PAR bZip transcription factors results in epilepsy. Genes
Dev. 18: 1397-1412, 2004.
3. Hanna, M. C.; Turner, A. J.; Kirkness, E. F.: Human pyridoxal
kinase: cDNA cloning, expression, and modulation by ligands of the
benzodiazepine receptor. J. Biol. Chem. 272: 10756-10760, 1997.
4. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
*FIELD* CN
Patricia A. Hartz - updated: 7/2/2004
Jennifer P. Macke - updated: 3/12/1999
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 08/05/2004
terry: 7/2/2004
mgross: 3/15/1999
mgross: 3/12/1999
warfield: 3/7/1994
supermim: 3/16/1992
carol: 3/5/1992
carol: 2/26/1991
carol: 2/8/1991
supermim: 3/20/1990
*RECORD*
*FIELD* NO
179020
*FIELD* TI
*179020 PYRIDOXAL KINASE; PDXK
;;PYRIDOXINE KINASE; PNK;;
PKH;;
VITAMIN B6 KINASE
*FIELD* TX
read more
DESCRIPTION
Pyridoxal kinase (PDXK; EC 2.7.1.35) converts vitamin B6 to
pyridoxal-5-phosphate (PLP), an essential cofactor in the intermediate
metabolism of amino acids and neurotransmitters.
CLONING
Hanna et al. (1997) cloned the cDNA encoding PDXK, which they referred
to as PKH. The PDXK gene encodes a 312-amino acid polypeptide, and
expression of the cDNA revealed pyridoxal kinase activity. Northern blot
analysis revealed that a major 1.5-kb PDXK transcript was expressed in
all tissues tested.
GENE FUNCTION
The expression of PDXK shows circadian oscillations. Gachon et al.
(2004) found that the expression of Pdxk in mouse liver and brain is
regulated by the 3 PAR bZIP transcription factors, Dbp (124097), Hlf
(142385), and Tef (179020), which also show circadian oscillations in
expression. Mice devoid of all 3 transcription factors showed decreased
levels of brain PLP, serotonin, and dopamine, and were highly
susceptible to generalized spontaneous and audiogenic epilepsies that
were frequently lethal.
MAPPING
Hanna et al. (1997) reported that a BAC clone from the human 21q22.3
region contains almost the entire PDXK gene on 10 distinct exons.
MOLECULAR GENETICS
Chern and Beutler (1976) concluded that alleles at a locus symbolized
PNK determine the level of activity of pyridoxine kinase in
erythrocytes: PNK(H) and PNK(L), for 'high' and 'low', respectively. The
frequency of these 2 alleles was estimated to be 0.81 and 0.19 for
whites and 0.35 and 0.65 for blacks. They suggested that the PNK(L)
state of red cells is the result of a stability mutation.
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* RF
1. Chern, C. J.; Beutler, E.: Biochemical and electrophoretic studies
of erythrocyte pyridoxine kinase in white and black Americans. Am.
J. Hum. Genet. 28: 9-17, 1976.
2. Gachon, F.; Fonjallaz, P.; Damiola, F.; Gos, P.; Kodama, T.; Zakany,
J.; Duboule, D.; Petit, B.; Tafti, M.; Schibler, U.: The loss of
circadian PAR bZip transcription factors results in epilepsy. Genes
Dev. 18: 1397-1412, 2004.
3. Hanna, M. C.; Turner, A. J.; Kirkness, E. F.: Human pyridoxal
kinase: cDNA cloning, expression, and modulation by ligands of the
benzodiazepine receptor. J. Biol. Chem. 272: 10756-10760, 1997.
4. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
*FIELD* CN
Patricia A. Hartz - updated: 7/2/2004
Jennifer P. Macke - updated: 3/12/1999
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
carol: 08/05/2004
terry: 7/2/2004
mgross: 3/15/1999
mgross: 3/12/1999
warfield: 3/7/1994
supermim: 3/16/1992
carol: 3/5/1992
carol: 2/26/1991
carol: 2/8/1991
supermim: 3/20/1990