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Protein

[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial

Gene

Pdk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism.

Catalytic activityi

ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei294 – 2941ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi253 – 2608ATPBy similarity
Nucleotide bindingi313 – 3142ATPBy similarity
Nucleotide bindingi330 – 3356ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-DME-5362517. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial (EC:2.7.11.2)
Short name:
DmPDK
Short name:
Pyruvate dehydrogenase kinase
Gene namesi
Name:Pdk
ORF Names:CG8808
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0017558. Pdk.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 413[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrialPRO_0000023451
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

PaxDbiP91622.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiP91622.
ExpressionAtlasiP91622. differential.
GenevisibleiP91622. DM.

Interactioni

Protein-protein interaction databases

BioGridi61801. 4 interactions.
MINTiMINT-817309.
STRINGi7227.FBpp0111805.

Structurei

3D structure databases

ProteinModelPortaliP91622.
SMRiP91622. Positions 20-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini137 – 369233Histidine kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the PDK/BCKDK protein kinase family.Curated
Contains 1 histidine kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0787. Eukaryota.
COG0642. LUCA.
GeneTreeiENSGT00550000074574.
InParanoidiP91622.
OrthoDBiEOG71VSSV.
PhylomeDBiP91622.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
[Graphical view]
PfamiPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P91622-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLFPVRFSA ASSSMASLAK MLDFYSGFNP SPLSIKQFMD FGQNACEKKS
60 70 80 90 100
YIFLRKELPV RLANIMKEIA LLPDNLLHTR SVSEVSSWYV KSFEDVLVYE
110 120 130 140 150
KAEPTHDNLQ KFVADLDLIR NRHNDVVQTM AQGVIEMKEN EGGQVDAPTE
160 170 180 190 200
SSIQYFLDRL YMSRISIRML INQHTLLFGG NPHAGGRHIG CLDPACDLSD
210 220 230 240 250
VVRDAYENAR FLCDQYYLTS PALEIQQHSS EPGDNLPIRT VYVPSHLYYM
260 270 280 290 300
LFELFKNSMR AVVEHHGHDN NDTLPPLKVA ICKGKEDICV KISDQGGGIP
310 320 330 340 350
RSQTDQLFKY MYSTAPQPSK SDLHTVPLAG YGYGLPISRL YARYFHGDIV
360 370 380 390 400
LLSCEGFGTD AIIYLKALSD EANELLPIFN KTSSKFYRAT VPTGDWSNQV
410
KYAKKKKTSA VNQ
Length:413
Mass (Da):46,626
Last modified:August 16, 2005 - v2
Checksum:iAB8F1A5A61047D81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131S → L in BAA13724 (PubMed:9115642).Curated
Sequence conflicti412 – 4121N → S in BAA13724 (PubMed:9115642).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88814 mRNA. Translation: BAA13724.1.
AE013599 Genomic DNA. Translation: AAF58938.1.
AY075385 mRNA. Translation: AAL68223.1.
RefSeqiNP_001246224.1. NM_001259295.2.
NP_477215.1. NM_057867.4.
UniGeneiDm.7142.

Genome annotation databases

EnsemblMetazoaiFBtr0088508; FBpp0087592; FBgn0017558.
FBtr0306807; FBpp0297719; FBgn0017558.
GeneIDi35970.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88814 mRNA. Translation: BAA13724.1.
AE013599 Genomic DNA. Translation: AAF58938.1.
AY075385 mRNA. Translation: AAL68223.1.
RefSeqiNP_001246224.1. NM_001259295.2.
NP_477215.1. NM_057867.4.
UniGeneiDm.7142.

3D structure databases

ProteinModelPortaliP91622.
SMRiP91622. Positions 20-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61801. 4 interactions.
MINTiMINT-817309.
STRINGi7227.FBpp0111805.

Proteomic databases

PaxDbiP91622.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088508; FBpp0087592; FBgn0017558.
FBtr0306807; FBpp0297719; FBgn0017558.
GeneIDi35970.

Organism-specific databases

CTDi35970.
FlyBaseiFBgn0017558. Pdk.

Phylogenomic databases

eggNOGiKOG0787. Eukaryota.
COG0642. LUCA.
GeneTreeiENSGT00550000074574.
InParanoidiP91622.
OrthoDBiEOG71VSSV.
PhylomeDBiP91622.

Enzyme and pathway databases

ReactomeiR-DME-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-DME-5362517. Signaling by Retinoic Acid.

Miscellaneous databases

ChiTaRSiPdk1. fly.
GenomeRNAii35970.
NextBioi796101.
PROiP91622.

Gene expression databases

BgeeiP91622.
ExpressionAtlasiP91622. differential.
GenevisibleiP91622. DM.

Family and domain databases

Gene3Di1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProiIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_C.
IPR005467. His_kinase_dom.
[Graphical view]
PfamiPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEiPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPDK_DROME
AccessioniPrimary (citable) accession number: P91622
Secondary accession number(s): Q9V580
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: August 16, 2005
Last modified: May 11, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.