PDK_DROME
ID PDK_DROME Reviewed; 413 AA.
AC P91622; Q9V580;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial;
DE Short=DmPDK;
DE Short=Pyruvate dehydrogenase kinase;
DE EC=2.7.11.2;
DE Flags: Precursor;
GN Name=Pdk; ORFNames=CG8808;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=9115642; DOI=10.1089/dna.1997.16.335;
RA Katsube T., Nomoto S., Togashi S., Ueda R., Kobayashi M., Takahisa M.;
RT "cDNA sequence and expression of a gene encoding a pyruvate dehydrogenase
RT kinase homolog of Drosophila melanogaster.";
RL DNA Cell Biol. 16:335-339(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase complex by
CC phosphorylation of the E1 alpha subunit, thus contributing to the
CC regulation of glucose metabolism.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP
CC + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit];
CC Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9115642}.
CC -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC {ECO:0000305}.
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DR EMBL; D88814; BAA13724.1; -; mRNA.
DR EMBL; AE013599; AAF58938.1; -; Genomic_DNA.
DR EMBL; AY075385; AAL68223.1; -; mRNA.
DR RefSeq; NP_001246224.1; NM_001259295.2.
DR RefSeq; NP_477215.1; NM_057867.4.
DR AlphaFoldDB; P91622; -.
DR SMR; P91622; -.
DR BioGRID; 61801; 5.
DR STRING; 7227.FBpp0111805; -.
DR PaxDb; P91622; -.
DR DNASU; 35970; -.
DR EnsemblMetazoa; FBtr0088508; FBpp0087592; FBgn0017558.
DR EnsemblMetazoa; FBtr0306807; FBpp0297719; FBgn0017558.
DR GeneID; 35970; -.
DR KEGG; dme:Dmel_CG8808; -.
DR CTD; 35970; -.
DR FlyBase; FBgn0017558; Pdk.
DR VEuPathDB; VectorBase:FBgn0017558; -.
DR eggNOG; KOG0787; Eukaryota.
DR GeneTree; ENSGT01030000234646; -.
DR HOGENOM; CLU_023861_1_0_1; -.
DR InParanoid; P91622; -.
DR OMA; TIKHYSN; -.
DR OrthoDB; 1242599at2759; -.
DR PhylomeDB; P91622; -.
DR Reactome; R-DME-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-DME-5362517; Signaling by Retinoic Acid.
DR BioGRID-ORCS; 35970; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pdk; fly.
DR GenomeRNAi; 35970; -.
DR PRO; PR:P91622; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0017558; Expressed in adult Malpighian tubule (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P91622; baseline and differential.
DR Genevisible; P91622; DM.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:FlyBase.
DR GO; GO:0004740; F:pyruvate dehydrogenase (acetyl-transferring) kinase activity; ISS:FlyBase.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISS:FlyBase.
DR Gene3D; 1.20.140.20; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036784; AK/P_DHK_N_sf.
DR InterPro; IPR018955; BCDHK/PDK_N.
DR InterPro; IPR039028; BCKD/PDK.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR11947; PTHR11947; 1.
DR Pfam; PF10436; BCDHK_Adom3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF69012; SSF69012; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..413
FT /note="[Pyruvate dehydrogenase (acetyl-transferring)]
FT kinase, mitochondrial"
FT /id="PRO_0000023451"
FT DOMAIN 137..369
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 253..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 313..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 330..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="S -> L (in Ref. 1; BAA13724)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="N -> S (in Ref. 1; BAA13724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46626 MW; AB8F1A5A61047D81 CRC64;
MRLFPVRFSA ASSSMASLAK MLDFYSGFNP SPLSIKQFMD FGQNACEKKS YIFLRKELPV
RLANIMKEIA LLPDNLLHTR SVSEVSSWYV KSFEDVLVYE KAEPTHDNLQ KFVADLDLIR
NRHNDVVQTM AQGVIEMKEN EGGQVDAPTE SSIQYFLDRL YMSRISIRML INQHTLLFGG
NPHAGGRHIG CLDPACDLSD VVRDAYENAR FLCDQYYLTS PALEIQQHSS EPGDNLPIRT
VYVPSHLYYM LFELFKNSMR AVVEHHGHDN NDTLPPLKVA ICKGKEDICV KISDQGGGIP
RSQTDQLFKY MYSTAPQPSK SDLHTVPLAG YGYGLPISRL YARYFHGDIV LLSCEGFGTD
AIIYLKALSD EANELLPIFN KTSSKFYRAT VPTGDWSNQV KYAKKKKTSA VNQ
