LOCUS AEE78913.1 713 aa PRT PLN 23-MAR-2023 DEFINITION Arabidopsis thaliana Dihydrolipoamide acetyltransferase, long form protein protein. ACCESSION CP002686-7319 PROTEIN_ID AEE78913.1 SOURCE Arabidopsis thaliana (thale cress) ORGANISM Arabidopsis thaliana Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. REFERENCE 1 (bases 1 to 23459830) AUTHORS Salanoubat,M., Lemcke,K., Rieger,M., Ansorge,W., Unseld,M., Fartmann,B., Valle,G., Blocker,H., Perez-Alonso,M., Obermaier,B., Delseny,M., Boutry,M., Grivell,L.A., Mache,R., Puigdomenech,P., De Simone,V., Choisne,N., Artiguenave,F., Robert,C., Brottier,P., Wincker,P., Cattolico,L., Weissenbach,J., Saurin,W., Quetier,F., Schafer,M., Muller-Auer,S., Gabel,C., Fuchs,M., Benes,V., Wurmbach,E., Drzonek,H., Erfle,H., Jordan,N., Bangert,S., Wiedelmann,R., Kranz,H., Voss,H., Holland,R., Brandt,P., Nyakatura,G., Vezzi,A., D'Angelo,M., Pallavicini,A., Toppo,S., Simionati,B., Conrad,A., Hornischer,K., Kauer,G., Lohnert,T.H., Nordsiek,G., Reichelt,J., Scharfe,M., Schon,O., Bargues,M., Terol,J., Climent,J., Navarro,P., Collado,C., Perez-Perez,A., Ottenwalder,B., Duchemin,D., Cooke,R., Laudie,M., Berger-Llauro,C., Purnelle,B., Masuy,D., de Haan,M., Maarse,A.C., Alcaraz,J.P., Cottet,A., Casacuberta,E., Monfort,A., Argiriou,A., flores,M., Liguori,R., Vitale,D., Mannhaupt,G., Haase,D., Schoof,H., Rudd,S., Zaccaria,P., Mewes,H.W., Mayer,K.F., Kaul,S., Town,C.D., Koo,H.L., Tallon,L.J., Jenkins,J., Rooney,T., Rizzo,M., Walts,A., Utterback,T., Fujii,C.Y., Shea,T.P., Creasy,T.H., Haas,B., Maiti,R., Wu,D., Peterson,J., Van Aken,S., Pai,G., Militscher,J., Sellers,P., Gill,J.E., Feldblyum,T.V., Preuss,D., Lin,X., Nierman,W.C., Salzberg,S.L., White,O., Venter,J.C., Fraser,C.M., Kaneko,T., Nakamura,Y., Sato,S., Kato,T., Asamizu,E., Sasamoto,S., Kimura,T., Idesawa,K., Kawashima,K., Kishida,Y., Kiyokawa,C., Kohara,M., Matsumoto,M., Matsuno,A., Muraki,A., Nakayama,S., Nakazaki,N., Shinpo,S., Takeuchi,C., Wada,T., Watanabe,A., Yamada,M., Yasuda,M. and Tabata,S. CONSRTM European Union Chromosome 3 Arabidopsis Sequencing Consortium; Institute for Genomic Research; Kazusa DNA Research Institute TITLE Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana JOURNAL Nature 408 (6814), 820-822 (2000) PUBMED 11130713 REFERENCE 2 (bases 1 to 23459830) AUTHORS Swarbreck,D., Lamesch,P., Wilks,C. and Huala,E. CONSRTM TAIR TITLE Direct Submission JOURNAL Submitted (18-FEB-2011) Department of Plant Biology, Carnegie Institution, 260 Panama Street, Stanford, CA, USA REFERENCE 3 (bases 1 to 23459830) AUTHORS Krishnakumar,V., Cheng,C.-Y., Chan,A.P., Schobel,S., Kim,M., Ferlanti,E.S., Belyaeva,I., Rosen,B.D., Micklem,G., Miller,J.R., Vaughn,M. and Town,C.D. TITLE Direct Submission JOURNAL Submitted (17-MAY-2016) Plant Genomics, J. Craig Venter Institute, 9704 Medical Center Dr, Rockville, MD 20850, USA REMARK Protein update by submitter FEATURES Qualifiers source /organism="Arabidopsis thaliana" /mol_type="genomic DNA" /db_xref="taxon:3702" /chromosome="3" /ecotype="Columbia" protein /gene="LTA3" /locus_tag="AT3G52200" /gene_synonym="DIHYDROLIPOAMIDE S-ACETYLTRANSFERASE" /note="LTA3; FUNCTIONS IN: dihydrolipoyllysine-residue acetyltransferase activity; INVOLVED IN: pyruvate metabolic process, metabolic process; LOCATED IN: mitochondrion; EXPRESSED IN: 24 plant structures; EXPRESSED DURING: 13 growth stages; CONTAINS InterPro DOMAIN/s: 2-oxo acid dehydrogenase, lipoyl-binding site (InterPro:IPR003016), Dihydrolipoamide acetyltransferase, long form (InterPro:IPR006257), E3 binding (InterPro:IPR004167), 2-oxoacid dehydrogenase acyltransferase, catalytic domain (InterPro:IPR001078), Single hybrid motif (InterPro:IPR011053), Biotin/lipoyl attachment (InterPro:IPR000089); BEST Arabidopsis thaliana protein match is: Dihydrolipoamide acetyltransferase, long form protein (TAIR:AT1G54220.2)." /db_xref="TAIR:AT3G52200" /db_xref="Araport:AT3G52200" intron_pos 32:2 (1/22) intron_pos 51:2 (2/22) intron_pos 70:0 (3/22) intron_pos 81:1 (4/22) intron_pos 174:0 (5/22) intron_pos 189:0 (6/22) intron_pos 213:2 (7/22) intron_pos 237:0 (8/22) intron_pos 301:0 (9/22) intron_pos 316:0 (10/22) intron_pos 340:2 (11/22) intron_pos 364:0 (12/22) intron_pos 494:0 (13/22) intron_pos 514:1 (14/22) intron_pos 529:1 (15/22) intron_pos 557:1 (16/22) intron_pos 583:0 (17/22) intron_pos 604:0 (18/22) intron_pos 627:2 (19/22) intron_pos 648:0 (20/22) intron_pos 668:1 (21/22) intron_pos 695:1 (22/22) BEGIN 1 MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV RSASIDLITR 61 MDDSSPKPIL RFGVQNFSST AIRLTNTDVK WVIRIINGNF RLTCRKIEML IDAGAKTSIS 121 LFSLMFVLPS YLRYSDRRCN QLYKILPLNY YFLWVVGPIS QTVLAMPALS PTMSHGNVVK 181 WMKKEGDKVE VGDVLCEIET DKATVEFESQ EEGFLAKILV TEGSKDIPVN EPIAIMVEEE 241 DDIKNVPATI EGGRDGKEET SAHQVMKPDE STQQKSSIQP DASDLPPHVV LEMPALSPTM 301 NQGNIAKWWK KEGDKIEVGD VIGEIETDKA TLEFESLEEG YLAKILIPEG SKDVAVGKPI 361 ALIVEDAESI EAIKSSSAGS SEVDTVKEVP DSVVDKPTER KAGFTKISPA AKLLILEHGL 421 EASSIEASGP YGTLLKSDVV AAIASGKASK SSASTKKKQP SKETPSKSSS TSKPSVTQSD 481 NNYEDFPNSQ IRKIIAKRLL ESKQKIPHLY LQSDVVLDPL LAFRKELQEN HGVKVSVNDI 541 VIKAVAVALR NVRQANAFWD AEKGDIVMCD SVDISIAVAT EKGLMTPIIK NADQKSISAI 601 SLEVKELAQK ARSGKLAPHE FQGGTFSISN LGMYPVDNFC AIINPPQAGI LAVGRGNKVV 661 EPVIGLDGIE KPSVVTKMNV TLSADHRIFD GQVGASFMSE LRSNFEDVRR LLL //