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Protein

Pyridoxal kinase

Gene

Pdxk

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • ATP binding Source: UniProtKB-KW
  • drug binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • pyridoxal binding Source: RGD
  • pyridoxal kinase activity Source: RGD

GO - Biological processi

  • negative regulation of apoptotic process Source: RGD
  • pyridoxal 5'-phosphate salvage Source: InterPro
  • pyridoxal phosphate biosynthetic process Source: RGD
  • response to amine Source: RGD
  • response to drug Source: RGD
  • response to food Source: RGD
  • response to insecticide Source: RGD
  • response to progesterone Source: RGD
  • response to toxic substance Source: RGD
  • response to X-ray Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.7.1.35. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal kinase (EC:2.7.1.35)
Alternative name(s):
Pyridoxine kinase
Gene namesi
Name:Pdxk
Synonyms:Pkh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621324. 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_0000213338Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO35331.
PRIDEiO35331.

PTM databases

iPTMnetiO35331.
PhosphoSiteiO35331.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001589.

Structurei

3D structure databases

ProteinModelPortaliO35331.
SMRiO35331. Positions 1-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pyridoxine kinase family.Curated

Phylogenomic databases

eggNOGiKOG2599. Eukaryota.
COG2240. LUCA.
HOGENOMiHOG000258174.
HOVERGENiHBG000732.
InParanoidiO35331.
KOiK00868.
PhylomeDBiO35331.

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.

O35331-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA
60 70 80 90 100
HWKGQVLTSQ ELHALYEGLK ANNVNKYDYV LTGYTRDKSF LGMVVDIVQE
110 120 130 140 150
LKQQNSRLVY VCDPVMGDKW NGEGSMYVPQ DLLPVYREKV VPMADIITPN
160 170 180 190 200
QFEAELLSGR KIHSQEEAFA VMDVLHRMGP DTVVITSSDL PSPKGSDYLM
210 220 230 240 250
ALGSQRMRKP DGSTVTQRIR MEMRKVDPVF VGTGDLFAAM LLAWTHKHPD
260 270 280 290 300
NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSRKDI
310
EDPEIVVQAT VL
Length:312
Mass (Da):34,908
Last modified:January 1, 1998 - v1
Checksum:i34C27148122268ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020346 mRNA. Translation: AAB71400.1.
RefSeqiNP_113957.1. NM_031769.1.
UniGeneiRn.18815.

Genome annotation databases

GeneIDi83578.
KEGGirno:83578.
UCSCiRGD:621324. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020346 mRNA. Translation: AAB71400.1.
RefSeqiNP_113957.1. NM_031769.1.
UniGeneiRn.18815.

3D structure databases

ProteinModelPortaliO35331.
SMRiO35331. Positions 1-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001589.

PTM databases

iPTMnetiO35331.
PhosphoSiteiO35331.

Proteomic databases

PaxDbiO35331.
PRIDEiO35331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83578.
KEGGirno:83578.
UCSCiRGD:621324. rat.

Organism-specific databases

CTDi8566.
RGDi621324. Pdxk.

Phylogenomic databases

eggNOGiKOG2599. Eukaryota.
COG2240. LUCA.
HOGENOMiHOG000258174.
HOVERGENiHBG000732.
InParanoidiO35331.
KOiK00868.
PhylomeDBiO35331.

Enzyme and pathway databases

BRENDAi2.7.1.35. 5301.

Miscellaneous databases

PROiO35331.

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

  1. Wu Y., Ngo E., Nutter L.M.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 77-102; 161-177 AND 276-292, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiPDXK_RAT
AccessioniPrimary (citable) accession number: O35331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 104 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. 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.