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Protein

Pyridoxal kinase

Gene

PDXK

Organism
Ovis aries (Sheep)
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.

Catalytic activityi

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

Cofactori

Zn2+, Mg2+Note: Divalent metal cations. Zn2+ is more efficient than Mg2+.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121Substrate1 Publication
Binding sitei47 – 471Substrate1 Publication
Binding sitei127 – 1271Substrate1 Publication
Binding sitei235 – 2351Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi186 – 1872ATP1 Publication
Nucleotide bindingi223 – 23412ATP1 PublicationAdd
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

BRENDAi2.7.1.35. 2668.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal kinase (EC:2.7.1.35)
Alternative name(s):
Pyridoxine kinase
Gene namesi
Name:PDXK
Synonyms:PKH
OrganismiOvis aries (Sheep)
Taxonomic identifieri9940 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis
Proteomesi
  • UP000002356 Componenti: Unplaced

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_0000213339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei164 – 1641PhosphoserineBy similarity
Modified residuei213 – 2131PhosphoserineBy similarity
Modified residuei285 – 2851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1712Combined sources
Helixi21 – 3010Combined sources
Beta strandi34 – 4512Combined sources
Beta strandi54 – 563Combined sources
Helixi59 – 7113Combined sources
Beta strandi78 – 825Combined sources
Helixi88 – 10417Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi125 – 1284Combined sources
Helixi130 – 1323Combined sources
Helixi133 – 1386Combined sources
Helixi141 – 1433Combined sources
Beta strandi145 – 1473Combined sources
Helixi151 – 1588Combined sources
Helixi165 – 17814Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi198 – 20710Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi215 – 22410Combined sources
Helixi233 – 24715Combined sources
Helixi252 – 27726Combined sources
Beta strandi280 – 2823Combined sources
Turni286 – 2894Combined sources
Helixi294 – 2963Combined sources
Helixi297 – 3015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LHPX-ray2.10A/B1-312[»]
1LHRX-ray2.60A/B1-312[»]
1RFTX-ray2.80A1-312[»]
1RFUX-ray2.80A/B/C/D/E/F/G/H1-312[»]
1RFVX-ray2.80A/B1-312[»]
1YGJX-ray2.70A1-312[»]
1YGKX-ray2.60A1-312[»]
1YHJX-ray2.80A1-312[»]
ProteinModelPortaliP82197.
SMRiP82197. Positions 1-312.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82197.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyridoxine kinase family.Curated

Phylogenomic databases

HOVERGENiHBG000732.
KOiK00868.

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.

P82197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEECRVLSI QSHVVRGYVG NRAATFPLQV LGFEVDAVNS VQFSNHTGYS
60 70 80 90 100
HWKGQVLNSD ELQELYDGLK LNHVNQYDYV LTGYTRDKSF LAMVVDIVQE
110 120 130 140 150
LKQQNPRLVY VCDPVMGDQR NGEGAMYVPD DLLPVYREKV VPVADIITPN
160 170 180 190 200
QFEAELLTGR KIHSQEEALE VMDMLHSMGP DTVVITSSNL LSPRGSDYLM
210 220 230 240 250
ALGSQRTRAP DGSVVTQRIR MEMHKVDAVF VGTGDLFAAM LLAWTHKHPN
260 270 280 290 300
NLKVACEKTV SAMHHVLQRT IKCAKAKSGE GVKPSPAQLE LRMVQSKKDI
310
ESPEIVVQAT VL
Length:312
Mass (Da):34,819
Last modified:May 30, 2000 - v1
Checksum:iC5F286DBCF51CA6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 4732RGYVG…FSNHT → MCFGGTAESLCPGDLMQHRG LTWSALPPTPPP (Ref. 2) CuratedAdd
BLAST
Sequence conflicti61 – 622EL → DV in AAD34353 (Ref. 2) Curated
Sequence conflicti189 – 1891N → D in AAD34353 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125374 mRNA. Translation: AAD34353.1.
RefSeqiNP_001009220.1. NM_001009220.1.
UniGeneiOar.696.

Genome annotation databases

GeneIDi443049.
KEGGioas:443049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125374 mRNA. Translation: AAD34353.1.
RefSeqiNP_001009220.1. NM_001009220.1.
UniGeneiOar.696.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LHPX-ray2.10A/B1-312[»]
1LHRX-ray2.60A/B1-312[»]
1RFTX-ray2.80A1-312[»]
1RFUX-ray2.80A/B/C/D/E/F/G/H1-312[»]
1RFVX-ray2.80A/B1-312[»]
1YGJX-ray2.70A1-312[»]
1YGKX-ray2.60A1-312[»]
1YHJX-ray2.80A1-312[»]
ProteinModelPortaliP82197.
SMRiP82197. Positions 1-312.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi443049.
KEGGioas:443049.

Organism-specific databases

CTDi8566.

Phylogenomic databases

HOVERGENiHBG000732.
KOiK00868.

Enzyme and pathway databases

BRENDAi2.7.1.35. 2668.

Miscellaneous databases

EvolutionaryTraceiP82197.

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. "Structure of pyridoxal kinase from sheep brain and role of the tryptophanyl residues."
    Maras B., Valiante S., Orru S., Simmaco M., Barra D., Churchich J.E.
    J. Protein Chem. 18:259-268(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE OF 113-259, ACETYLATION AT MET-1.
    Tissue: Brain.
  2. Kwon O.-S., Lee H.-S.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-312.
    Tissue: Liver.
  3. "Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain."
    Li M.-H., Kwok F., An X.-M., Chang W.-R., Lau C.-K., Zhang J.-P., Liu S.-Q., Leung Y.-C., Jiang T., Liang D.-C.
    Acta Crystallogr. D 58:1479-1481(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ATP.
  4. "Crystal structure of brain pyridoxal kinase, a novel member of the ribokinase superfamily."
    Li M.-H., Kwok F., Chang W.-R., Lau C.-K., Zhang J.-P., Lo S.C.L., Jiang T., Liang D.-C.
    J. Biol. Chem. 277:46385-46390(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; ADP AND COFACTOR.

Entry informationi

Entry nameiPDXK_SHEEP
AccessioniPrimary (citable) accession number: P82197
Secondary accession number(s): Q9XSD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 6, 2016
This is version 95 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.