Reviewed, UniProtKB/Swiss-Prot O02623 (PDK_ASCSU)

Names and origin

Protein names	Recommended name:     [Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial       Short name=Pyruvate dehydrogenase kinase     EC=2.7.11.2
Organism	Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier	6253 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism.
Catalytic activity	ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the PDK/BCKDK protein kinase family. Contains 1 histidine kinase domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate dehydrogenase (acetyl-transferring) kinase activity Inferred from electronic annotation. Source: EC two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 18	18	Mitochondrion Potential
	Chain	19 – 399	381	[Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial		PRO_0000023449
Regions
	Domain	123 – 360	238	Histidine kinase

Sequences

	Sequence		Length	Mass (Da)
	O02623-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 31F0EDA7D4F0412A	FASTA	399	45,402
	10 20 30 40 50 60 MFLTRRLLGP FTSAIARKLE HYSQFQPSSL TIQQYLDFGQ TGTMKSSFLF LKNELLVRLA 70 80 90 100 110 120 NIMQEISLLP PTLLKMPSRR LVSNWYCESF EDLLQFEHAQ VEPDIMSKFN DQLQTILKRH 130 140 150 160 170 180 SRVVETMAEG LIELRESEGV DIASERGIQY FLDRFYINRI SIRMLQNQHL VVFGVVLPES 190 200 210 220 230 240 PRHIGCIDPG CDVESVVHDA YENARFLCER YYLTAPGMKL EMHNSVNPGM PISIVAVPSH 250 260 270 280 290 300 LYHIMFELFK NSMRATVENH GADEDLPPIK VMVVRGAEDL SIKISDRGGG VSRTILDRLF 310 320 330 340 350 360 TYMYSTAPPP PRDGTQPPLA GYGYGLPLSR LYARYFHGDM YLVSMEGYGT DAMIFLKAIP 370 380 390 VEASEVLPIY STSSRRQLTM SPQAADWSHQ LPNHGNRNL

References

[1]

"Molecular cloning, functional expression, and characterization of pyruvate dehydrogenase kinase from anaerobic muscle of the parasitic nematode Ascaris suum." Chen W., Huang X., Komuniecki P.R., Komuniecki R. Arch. Biochem. Biophys. 353:181-189(1998) [PubMed: 9578613] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U94519 mRNA. Translation: AAB52573.1.
3D structure databases
HSSP	HSSP built from PDB template 1JM6 based on UniProtKB Q64536.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.11.2. 649.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. IPR018955. BCDHK/PDK_mit. IPR005467. Sig_transdc_His_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF10436. BCDHK_Adom3. 1 hit. PF02518. HATPase_c. 1 hit. [Graphical view]
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
PROSITE	PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDK_ASCSU

Accession

Primary (citable) accession number: O02623

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)