PDXK_MOUSE
ID PDXK_MOUSE Reviewed; 312 AA.
AC Q8K183; Q3TM83; Q8BJQ5;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pyridoxal kinase;
DE EC=2.7.1.35 {ECO:0000250|UniProtKB:O00764};
DE AltName: Full=Pyridoxine kinase;
GN Name=Pdxk {ECO:0000312|MGI:MGI:1351869}; Synonyms=Pkh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Hypothalamus, Lung, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 140-160, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). PLP is
CC the active form of vitamin B6, and acts as a cofactor for over 140
CC different enzymatic reactions (By similarity).
CC {ECO:0000250|UniProtKB:O00764}.
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:0000250|UniProtKB:P82197};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O00764};
CC -!- ACTIVITY REGULATION: Activity is increased in the presence of K(+)or
CC Na(+). {ECO:0000250|UniProtKB:O00764}.
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:0000250|UniProtKB:O00764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O00764}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. {ECO:0000305}.
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DR EMBL; AK039194; BAC30274.1; -; mRNA.
DR EMBL; AK080846; BAC38041.1; -; mRNA.
DR EMBL; AK145470; BAE26454.1; -; mRNA.
DR EMBL; AK166078; BAE38559.1; -; mRNA.
DR EMBL; AK166464; BAE38792.1; -; mRNA.
DR EMBL; BC027745; AAH27745.1; -; mRNA.
DR CCDS; CCDS23965.1; -.
DR RefSeq; NP_742146.1; NM_172134.2.
DR PDB; 6YJZ; X-ray; 2.45 A; A/B/C/D=1-312.
DR PDB; 6YK0; X-ray; 2.90 A; A/B/C/D=1-312.
DR PDB; 6YK1; X-ray; 2.40 A; A/B/C/D=1-312.
DR PDBsum; 6YJZ; -.
DR PDBsum; 6YK0; -.
DR PDBsum; 6YK1; -.
DR AlphaFoldDB; Q8K183; -.
DR SMR; Q8K183; -.
DR BioGRID; 229701; 9.
DR IntAct; Q8K183; 3.
DR STRING; 10090.ENSMUSP00000038540; -.
DR iPTMnet; Q8K183; -.
DR PhosphoSitePlus; Q8K183; -.
DR SwissPalm; Q8K183; -.
DR EPD; Q8K183; -.
DR jPOST; Q8K183; -.
DR MaxQB; Q8K183; -.
DR PaxDb; Q8K183; -.
DR PeptideAtlas; Q8K183; -.
DR PRIDE; Q8K183; -.
DR ProteomicsDB; 289338; -.
DR Antibodypedia; 24020; 344 antibodies from 27 providers.
DR DNASU; 216134; -.
DR Ensembl; ENSMUST00000041616; ENSMUSP00000038540; ENSMUSG00000032788.
DR GeneID; 216134; -.
DR KEGG; mmu:216134; -.
DR UCSC; uc007fxu.2; mouse.
DR CTD; 8566; -.
DR MGI; MGI:1351869; Pdxk.
DR VEuPathDB; HostDB:ENSMUSG00000032788; -.
DR eggNOG; KOG2599; Eukaryota.
DR GeneTree; ENSGT00390000003874; -.
DR HOGENOM; CLU_046496_1_1_1; -.
DR InParanoid; Q8K183; -.
DR OMA; CPNQLEL; -.
DR OrthoDB; 1091630at2759; -.
DR PhylomeDB; Q8K183; -.
DR TreeFam; TF315004; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-964975; Vitamins B6 activation to pyridoxal phosphate.
DR UniPathway; UPA01068; UER00298.
DR UniPathway; UPA01068; UER00299.
DR UniPathway; UPA01068; UER00300.
DR BioGRID-ORCS; 216134; 11 hits in 74 CRISPR screens.
DR ChiTaRS; Pdxk; mouse.
DR PRO; PR:Q8K183; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K183; protein.
DR Bgee; ENSMUSG00000032788; Expressed in cleaving embryo and 274 other tissues.
DR Genevisible; Q8K183; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0031403; F:lithium ion binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0030955; F:potassium ion binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0070280; F:pyridoxal binding; ISO:MGI.
DR GO; GO:0008478; F:pyridoxal kinase activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0036094; F:small molecule binding; ISO:MGI.
DR GO; GO:0031402; F:sodium ion binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; ISO:MGI.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; ISO:MGI.
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; Reference proteome; Sodium;
KW Transferase; Zinc.
FT CHAIN 1..312
FT /note="Pyridoxal kinase"
FT /id="PRO_0000213336"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 12
FT /ligand="pyridoxal"
FT /ligand_id="ChEBI:CHEBI:17310"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 47
FT /ligand="pyridoxal"
FT /ligand_id="ChEBI:CHEBI:17310"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 47
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 113
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 148
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 150..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 186..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 186
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 226..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT BINDING 234..235
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O00764"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P82197"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 188
FT /note="S -> F (in Ref. 1; BAC38041)"
FT /evidence="ECO:0000305"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 88..104
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:6YK0"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6YK0"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:6YK1"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 252..277
FT /evidence="ECO:0007829|PDB:6YK1"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6YK1"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:6YK1"
SQ SEQUENCE 312 AA; 35015 MW; C4F32E8A27E751AF CRC64;
MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA HWKGQVLKSQ
ELHELYEGLK VNDVNKYDYV LTGYTRDKSF LAMVVDIVRE LKQQNSRLVY VCDPVMGDKW
NGEGSMYVPQ DLLPVYRDKV VPVADIITPN QFEAELLSGR KIHSQEEAFE VMDMLHCMGP
DTVVITSSDL PSSQGSDYLI ALGSQRMRKP DGSTVTQRIR MEMRKVEAVF VGTGDLFAAM
LLAWTHKHPD NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSKRDI
EDPEIVVQAT VL
