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   16-JUN-2009, entry version 53.
DE   RecName: Full=Pyridoxal kinase;
DE            EC=2.7.1.35;
DE   AltName: Full=Pyridoxine kinase;
GN   Name=Pdxk; Synonyms=Pkh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 140-160, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Required for synthesis of pyridoxal-5-phosphate from
CC       vitamin B6 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate.
CC   -!- COFACTOR: Divalent cations. Zinc is more efficient than magnesium
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
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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   IPI; IPI00283511; -.
DR   RefSeq; NP_742146.1; -.
DR   UniGene; Mm.206159; -.
DR   HSSP; P82197; 1LHP.
DR   SMR; Q8K183; 4-312.
DR   PRIDE; Q8K183; -.
DR   Ensembl; ENSMUSG00000032788; Mus musculus.
DR   GeneID; 216134; -.
DR   KEGG; mmu:216134; -.
DR   NMPDR; fig|10090.3.peg.13944; -.
DR   MGI; MGI:1351869; Pdxk.
DR   HOGENOM; Q8K183; -.
DR   HOVERGEN; Q8K183; -.
DR   OMA; Q8K183; CAKAQAG.
DR   BRENDA; 2.7.1.35; 244.
DR   NextBio; 374990; -.
DR   ArrayExpress; Q8K183; -.
DR   Bgee; Q8K183; -.
DR   CleanEx; MM_PDXK; -.
DR   GermOnline; ENSMUSG00000032788; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR011611; Carb/pur_kinase.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF00294; PfkB; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Transferase; Zinc.
FT   CHAIN         1    312       Pyridoxal kinase.
FT                                /FTId=PRO_0000213336.
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     213    213       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   CONFLICT    188    188       S -> F (in Ref. 1; BAC38041).
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
//