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Protein

Pyridoxal kinase

Gene

Pdxk

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for synthesis of pyridoxal-5-phosphate from vitamin B6.By similarity

Catalytic activityi

ATP + pyridoxal = ADP + pyridoxal 5'-phosphate.

Cofactori

Zn2+By similarity, Mg2+By similarityNote: Divalent metal cations. Zn2+ is more efficient than Mg2+.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121SubstrateBy similarity
Binding sitei47 – 471SubstrateBy similarity
Binding sitei127 – 1271SubstrateBy similarity
Binding sitei235 – 2351SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi186 – 1872ATPBy similarity
Nucleotide bindingi223 – 23412ATPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-964975. Vitamins B6 activation to pyridoxal phosphate.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal kinase (EC:2.7.1.35)
Alternative name(s):
Pyridoxine kinase
Gene namesi
Name:Pdxk
Synonyms:Pkh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1351869. Pdxk.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Pyridoxal kinasePRO_0000213336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei59 – 591PhosphoserineCombined sources
Modified residuei164 – 1641PhosphoserineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei285 – 2851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8K183.
MaxQBiQ8K183.
PaxDbiQ8K183.
PRIDEiQ8K183.

PTM databases

iPTMnetiQ8K183.
PhosphoSiteiQ8K183.
SwissPalmiQ8K183.

Expressioni

Gene expression databases

BgeeiQ8K183.
CleanExiMM_PDXK.
ExpressionAtlasiQ8K183. baseline and differential.
GenevisibleiQ8K183. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229701. 1 interaction.
IntActiQ8K183. 4 interactions.
MINTiMINT-1854852.
STRINGi10090.ENSMUSP00000038540.

Structurei

3D structure databases

ProteinModelPortaliQ8K183.
SMRiQ8K183. Positions 4-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyridoxine kinase family.Curated

Phylogenomic databases

eggNOGiKOG2599. Eukaryota.
COG2240. LUCA.
GeneTreeiENSGT00390000003874.
HOGENOMiHOG000258174.
HOVERGENiHBG000732.
InParanoidiQ8K183.
KOiK00868.
OMAiRIRMEMH.
OrthoDBiEOG70088R.
PhylomeDBiQ8K183.
TreeFamiTF315004.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR013749. PM/HMP-P_kinase-1.
IPR004625. PyrdxlKinase.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERiPTHR10534. PTHR10534. 1 hit.
PfamiPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00687. pyridox_kin. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8K183-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA
60 70 80 90 100
HWKGQVLKSQ ELHELYEGLK VNDVNKYDYV LTGYTRDKSF LAMVVDIVRE
110 120 130 140 150
LKQQNSRLVY VCDPVMGDKW NGEGSMYVPQ DLLPVYRDKV VPVADIITPN
160 170 180 190 200
QFEAELLSGR KIHSQEEAFE VMDMLHCMGP DTVVITSSDL PSSQGSDYLI
210 220 230 240 250
ALGSQRMRKP DGSTVTQRIR MEMRKVEAVF VGTGDLFAAM LLAWTHKHPD
260 270 280 290 300
NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSKRDI
310
EDPEIVVQAT VL
Length:312
Mass (Da):35,015
Last modified:October 1, 2002 - v1
Checksum:iC4F32E8A27E751AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881S → F in BAC38041 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23965.1.
RefSeqiNP_742146.1. NM_172134.2.
UniGeneiMm.206159.

Genome annotation databases

EnsembliENSMUST00000041616; ENSMUSP00000038540; ENSMUSG00000032788.
GeneIDi216134.
KEGGimmu:216134.
UCSCiuc007fxu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23965.1.
RefSeqiNP_742146.1. NM_172134.2.
UniGeneiMm.206159.

3D structure databases

ProteinModelPortaliQ8K183.
SMRiQ8K183. Positions 4-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229701. 1 interaction.
IntActiQ8K183. 4 interactions.
MINTiMINT-1854852.
STRINGi10090.ENSMUSP00000038540.

PTM databases

iPTMnetiQ8K183.
PhosphoSiteiQ8K183.
SwissPalmiQ8K183.

Proteomic databases

EPDiQ8K183.
MaxQBiQ8K183.
PaxDbiQ8K183.
PRIDEiQ8K183.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041616; ENSMUSP00000038540; ENSMUSG00000032788.
GeneIDi216134.
KEGGimmu:216134.
UCSCiuc007fxu.2. mouse.

Organism-specific databases

CTDi8566.
MGIiMGI:1351869. Pdxk.

Phylogenomic databases

eggNOGiKOG2599. Eukaryota.
COG2240. LUCA.
GeneTreeiENSGT00390000003874.
HOGENOMiHOG000258174.
HOVERGENiHBG000732.
InParanoidiQ8K183.
KOiK00868.
OMAiRIRMEMH.
OrthoDBiEOG70088R.
PhylomeDBiQ8K183.
TreeFamiTF315004.

Enzyme and pathway databases

ReactomeiR-MMU-964975. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

ChiTaRSiPdxk. mouse.
NextBioi374990.
PROiQ8K183.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K183.
CleanExiMM_PDXK.
ExpressionAtlasiQ8K183. baseline and differential.
GenevisibleiQ8K183. MM.

Family and domain databases

Gene3Di3.40.1190.20. 1 hit.
InterProiIPR013749. PM/HMP-P_kinase-1.
IPR004625. PyrdxlKinase.
IPR029056. Ribokinase-like.
[Graphical view]
PANTHERiPTHR10534. PTHR10534. 1 hit.
PfamiPF08543. Phos_pyr_kin. 1 hit.
[Graphical view]
SUPFAMiSSF53613. SSF53613. 1 hit.
TIGRFAMsiTIGR00687. pyridox_kin. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPDXK_MOUSE
AccessioniPrimary (citable) accession number: Q8K183
Secondary accession number(s): Q3TM83, Q8BJQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.