Reviewed, UniProtKB/Swiss-Prot P91622 (PDK_DROME)

Names and origin

Protein names

Recommended name:
    [Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial
      Short name=Pyruvate dehydrogenase kinase
      Short name=DmPDK
    EC=2.7.11.2

Gene names

Name:	Pdk
ORF Names:	CG8808

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	413 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.
Developmental stage	Expressed both maternally and zygotically. Ref.1
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
Technical term	Complete proteome
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 – ?		Mitochondrion Potential
	Chain	? – 413		[Pyruvate dehydrogenase [lipoamide]] kinase, mitochondrial		PRO_0000023451
Regions
	Domain	137 – 369	233	Histidine kinase
Experimental info
	Sequence conflict	13	1	S → L in BAA13724. Ref.1
	Sequence conflict	412	1	N → S in BAA13724. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P91622-1 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: AB8F1A5A61047D81	FASTA	413	46,626
	10 20 30 40 50 60 MRLFPVRFSA ASSSMASLAK MLDFYSGFNP SPLSIKQFMD FGQNACEKKS YIFLRKELPV 70 80 90 100 110 120 RLANIMKEIA LLPDNLLHTR SVSEVSSWYV KSFEDVLVYE KAEPTHDNLQ KFVADLDLIR 130 140 150 160 170 180 NRHNDVVQTM AQGVIEMKEN EGGQVDAPTE SSIQYFLDRL YMSRISIRML INQHTLLFGG 190 200 210 220 230 240 NPHAGGRHIG CLDPACDLSD VVRDAYENAR FLCDQYYLTS PALEIQQHSS EPGDNLPIRT 250 260 270 280 290 300 VYVPSHLYYM LFELFKNSMR AVVEHHGHDN NDTLPPLKVA ICKGKEDICV KISDQGGGIP 310 320 330 340 350 360 RSQTDQLFKY MYSTAPQPSK SDLHTVPLAG YGYGLPISRL YARYFHGDIV LLSCEGFGTD 370 380 390 400 410 AIIYLKALSD EANELLPIFN KTSSKFYRAT VPTGDWSNQV KYAKKKKTSA VNQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence and expression of a gene encoding a pyruvate dehydrogenase kinase homolog of Drosophila melanogaster." Katsube T., Nomoto S., Togashi S., Ueda R., Kobayashi M., Takahisa M. DNA Cell Biol. 16:335-339(1997) [PubMed: 9115642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D88814 mRNA. Translation: BAA13724.1. AE013599 Genomic DNA. Translation: AAF58938.1. AY075385 mRNA. Translation: AAL68223.1.
RefSeq	NP_477215.1.
UniGene	Dm.7142
3D structure databases
HSSP	HSSP built from PDB template 1JM6 based on UniProtKB Q64536.
ModBase	Search...
Protein-protein interaction databases
IntAct	P91622. 4 interactions.
STRING	P91622.
Genome annotation databases
Ensembl	FBtr0112892; FBpp0111805; FBgn0017558; Drosophila melanogaster. [Genome view]
GeneID	35970.
NMPDR	fig|7227.3.peg.4078.
Organism-specific databases
CTD	35970.
FlyBase	FBgn0017558. Pdk.
Phylogenomic databases
HOGENOM	P91622.
OMA	ISYVPSH.
Enzyme and pathway databases
BRENDA	2.7.11.2. 48.
Gene expression databases
GermOnline	CG8808. Drosophila melanogaster.
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...
Other Resources
NextBio	796101.

Entry information

Entry name

PDK_DROME

Accession

Primary (citable) accession number: P91622
Secondary accession number(s): Q9V580

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	August 16, 2005
Last modified:	November 3, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project