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
//