Reviewed, UniProtKB/Swiss-Prot Q8K183 (PDXK_MOUSE)

Names and origin

Protein names

Recommended name:
    Pyridoxal kinase
    EC=2.7.1.35
Alternative name(s):
    Pyridoxine kinase

Gene names

Name:	Pdxk
Synonyms:	Pkh

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for synthesis of pyridoxal-5-phosphate from vitamin B6 By similarity.
Catalytic activity	ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.
Cofactor	Divalent cations. Zinc is more efficient than magnesium By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the pyridoxine kinase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal kinase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Pyridoxal kinase		PRO_0000213336
Regions
	Nucleotide binding	186 – 187	2	ATP By similarity
	Nucleotide binding	223 – 234	12	ATP By similarity
Sites
	Binding site	12	1	Substrate By similarity
	Binding site	47	1	Substrate By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	235	1	Substrate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	213	1	Phosphoserine By similarity
	Modified residue	285	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	188	1	S → F in BAC38041. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8K183-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: C4F32E8A27E751AF	FASTA	312	35,015
	10 20 30 40 50 60 MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA HWKGQVLKSQ 70 80 90 100 110 120 ELHELYEGLK VNDVNKYDYV LTGYTRDKSF LAMVVDIVRE LKQQNSRLVY VCDPVMGDKW 130 140 150 160 170 180 NGEGSMYVPQ DLLPVYRDKV VPVADIITPN QFEAELLSGR KIHSQEEAFE VMDMLHCMGP 190 200 210 220 230 240 DTVVITSSDL PSSQGSDYLI ALGSQRMRKP DGSTVTQRIR MEMRKVEAVF VGTGDLFAAM 250 260 270 280 290 300 LLAWTHKHPD NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSKRDI 310 EDPEIVVQAT VL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain, Hypothalamus, Lung and Mammary gland.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 140-160, MASS SPECTROMETRY. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK039194 mRNA. Translation: BAC30274.1. AK080846 mRNA. Translation: BAC38041.1. AK145470 mRNA. Translation: BAE26454.1. AK166078 mRNA. Translation: BAE38559.1. AK166464 mRNA. Translation: BAE38792.1. BC027745 mRNA. Translation: AAH27745.1.
IPI	IPI00283511.
RefSeq	NP_742146.1.
UniGene	Mm.206159
3D structure databases
HSSP	HSSP built from PDB template 1LHP based on UniProtKB P82197.
SMR	Q8K183. Positions 4-312.
ModBase	Search...
Proteomic databases
PRIDE	Q8K183.
Genome annotation databases
Ensembl	ENSMUSG00000032788. Mus musculus. [Contig view]
GeneID	216134.
KEGG	mmu:216134.
NMPDR	fig|10090.3.peg.13944.
Organism-specific databases
MGI	MGI:1351869. Pdxk.
Phylogenomic databases
HOGENOM	Q8K183.
HOVERGEN	Q8K183.
OMA	Q8K183. CAKAQAG.
Enzyme and pathway databases
BRENDA	2.7.1.35. 244.
Gene expression databases
ArrayExpress	Q8K183.
Bgee	Q8K183.
CleanEx	MM_PDXK.
GermOnline	ENSMUSG00000032788. Mus musculus.
Family and domain databases
InterPro	IPR011611. Carb/pur_kinase. IPR004625. PyrdxlP_synth_PyrdxlKinase. [Graphical view]
Pfam	PF00294. PfkB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00687. pyridox_kin. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	374990.
SOURCE	Search...

Entry information

Entry name

PDXK_MOUSE

Accession

Primary (citable) accession number: Q8K183
Secondary accession number(s): Q3TM83, Q8BJQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)