ID Q7YU05_DROME Unreviewed; 328 AA. AC Q7YU05; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 17-JUN-2020, entry version 149. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139}; DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139}; GN Name=Pdha {ECO:0000313|EMBL:AAF45978.1, GN ECO:0000313|FlyBase:FBgn0028325}; GN Synonyms=CG 7010 {ECO:0000313|EMBL:AAF45978.1}, Dmel\CG7010 GN {ECO:0000313|EMBL:AAF45978.1}, E1-PDH {ECO:0000313|EMBL:AAF45978.1}, l GN (1) G0334 {ECO:0000313|EMBL:AAF45978.1}, L(1)G0334 GN {ECO:0000313|EMBL:AAF45978.1}, L(1)g0334 GN {ECO:0000313|EMBL:AAF45978.1}, l(1)G0334 {ECO:0000313|EMBL:AAF45978.1, GN ECO:0000313|FlyBase:FBgn0028325}, PDH {ECO:0000313|EMBL:AAF45978.1}, GN Pdh {ECO:0000313|EMBL:AAF45978.1}, PDH-E1 GN {ECO:0000313|EMBL:AAF45978.1}, pdha {ECO:0000313|EMBL:AAF45978.1}, GN PDHalpha {ECO:0000313|EMBL:AAF45978.1}, PDHE1 GN {ECO:0000313|EMBL:AAF45978.1}; GN ORFNames=CG7010 {ECO:0000313|EMBL:AAQ22537.1, GN ECO:0000313|FlyBase:FBgn0028325}, Dmel_CG7010 GN {ECO:0000313|EMBL:AAF45978.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAQ22537.1}; RN [1] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., 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., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA 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] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAQ22537.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:AAQ22537.1}; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [8] {ECO:0000313|EMBL:AAF45978.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AAF45978.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [11] {ECO:0000313|EMBL:AAF45978.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [12] {ECO:0000313|EMBL:AAF45978.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [13] {ECO:0000313|EMBL:AAF45978.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [14] {ECO:0000313|EMBL:AAF45978.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). CC {ECO:0000256|RuleBase:RU361139}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)- CC lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue CC acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine + CC CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA- CC COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; CC Evidence={ECO:0000256|RuleBase:RU361139}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|RuleBase:RU361139}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014298; AAF45978.1; -; Genomic_DNA. DR EMBL; BT010068; AAQ22537.1; -; mRNA. DR RefSeq; NP_726947.1; NM_167019.2. DR IntAct; Q7YU05; 1. DR EnsemblMetazoa; FBtr0070710; FBpp0070678; FBgn0028325. DR GeneID; 31406; -. DR UCSC; CG7010-RB; d. melanogaster. DR CTD; 31406; -. DR FlyBase; FBgn0028325; Pdha. DR eggNOG; KOG0225; Eukaryota. DR eggNOG; COG1071; LUCA. DR GeneTree; ENSGT00530000063174; -. DR HOGENOM; CLU_029393_5_2_1; -. DR OMA; FGMPGVT; -. DR BioGRID-ORCS; 31406; 1 hit in 5 CRISPR screens. DR GenomeRNAi; 31406; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0028325; Expressed in arthropod fat body and 31 other tissues. DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central. DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y. DR InterPro; IPR029061; THDP-binding. DR Pfam; PF00676; E1_dh; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1. PE 1: Evidence at protein level; KW Oxidoreductase {ECO:0000256|RuleBase:RU361139, KW ECO:0000313|EMBL:AAF45978.1}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q7YU05}; KW Pyruvate {ECO:0000256|RuleBase:RU361139, ECO:0000313|EMBL:AAF45978.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU361139}. FT DOMAIN 1..291 FT /note="E1_dh" FT /evidence="ECO:0000259|Pfam:PF00676" SQ SEQUENCE 328 AA; 35895 MW; 1EDE726736F48768 CRC64; MQTIRRLETA AGNLYKEKII RGFCHLYSGQ EACAVGMKAA MRDVDNIISA YRVHGWTYLM GVSPSGVLAE LTGVQGGCAR GKGGSMHMYA PNFYGGNGIV GAQVPLGAGV GLACKYKGNG GMCLALYGDG AANQGQVFEA YNMAYLWKLP VIFVCENNNY GMGTSSERAS CNTDYYTRGD ALPGIWVDGM DVLAVRSATE FAINYVNTHG PLVMETNTYR YSGHSMSDPG TSYRTREEIQ EVRQKRDPIT SFKELCIELG LITTDEVKAI DLKVRKEVDE ATAFAKSDAE LGVSHLWTDV YSNNLEPKLR GTIAYDIDHI QERKGVNH //