ID ODO2A_ARATH Reviewed; 464 AA. AC Q9FLQ4; Q9ZRQ1; DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-JAN-2011, entry version 64. DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial; DE EC=2.3.1.61; DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2-1; DE Short=OGDC-E2-1; DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1; DE AltName: Full=E2K-1; DE Flags: Precursor; GN OrderedLocusNames=At5g55070; ORFNames=MCO15.2; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Machuy N., Klein M., Mueller-Roeber B.; RT "Cloning and characterization of 2-oxoglutarate dehydrogenase from RT Arabidopsis thaliana."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=cv. Landsberg erecta; RX PubMed=14671022; DOI=10.1105/tpc.016055; RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., RA Millar A.H.; RT "Experimental analysis of the Arabidopsis mitochondrial proteome RT highlights signaling and regulatory components, provides assessment of RT targeting prediction programs, and indicates plant-specific RT mitochondrial proteins."; RL Plant Cell 16:241-256(2004). CC -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the CC overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: 2- CC oxoglutarate dehydrogenase (E1), dihydrolipoamide CC succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By CC similarity). CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)- CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S- CC succinyldihydrolipoyl)lysine. CC -!- COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via CC saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. 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; AJ223803; CAA11553.1; -; mRNA. DR EMBL; AB010071; BAB08576.1; -; Genomic_DNA. DR EMBL; AY042897; AAK68837.1; -; mRNA. DR EMBL; AY128726; AAM91126.1; -; mRNA. DR IPI; IPI00531713; -. DR RefSeq; NP_200318.1; NM_124889.4. DR UniGene; At.20476; -. DR UniGene; At.71917; -. DR HSSP; P07016; 1C4T. DR ProteinModelPortal; Q9FLQ4; -. DR SMR; Q9FLQ4; 93-171, 235-464. DR STRING; Q9FLQ4; -. DR PRIDE; Q9FLQ4; -. DR EnsemblPlants; AT5G55070.1-TAIR; AT5G55070.1-P; AT5G55070-TAIR-G. DR GeneID; 835598; -. DR GenomeReviews; BA000015_GR; AT5G55070. DR KEGG; ath:AT5G55070; -. DR NMPDR; fig|3702.1.peg.27425; -. DR GeneFarm; 4414; -. DR TAIR; At5g55070; -. DR eggNOG; KOG0559; -. DR HOGENOM; HBG630916; -. DR InParanoid; Q9FLQ4; -. DR OMA; EDEILFE; -. DR PhylomeDB; Q9FLQ4; -. DR ArrayExpress; Q9FLQ4; -. DR Genevestigator; Q9FLQ4; -. DR GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR. DR GO; GO:0005739; C:mitochondrion; IDA:TAIR. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IDA:TAIR. DR GO; GO:0006979; P:response to oxidative stress; IDA:TAIR. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023213; CAT-like_dom. DR InterPro; IPR011053; Single_hybrid_motif. DR InterPro; IPR006255; SucB. DR Gene3D; G3DSA:3.30.559.10; G3DSA:3.30.559.10; 1. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR SUPFAM; SSF51230; Hybrid_motif; 1. DR TIGRFAMs; TIGR01347; sucB; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 1: Evidence at protein level; KW Acyltransferase; Complete proteome; Lipoyl; Mitochondrion; KW Transferase; Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1 86 Mitochondrion (Potential). FT CHAIN 87 464 Dihydrolipoyllysine-residue FT succinyltransferase component of 2- FT oxoglutarate dehydrogenase complex 1, FT mitochondrial. FT /FTId=PRO_0000399512. FT DOMAIN 94 167 Lipoyl-binding. FT COMPBIAS 179 231 Pro-rich. FT ACT_SITE 435 435 By similarity. FT ACT_SITE 439 439 By similarity. FT MOD_RES 134 134 N6-lipoyllysine (Potential). FT CONFLICT 30 34 VAVSA -> LVASS (in Ref. 1; CAA11553). FT CONFLICT 70 70 I -> V (in Ref. 1; CAA11553). FT CONFLICT 74 74 Y -> F (in Ref. 1; CAA11553). FT CONFLICT 218 219 Missing (in Ref. 1; CAA11553). SQ SEQUENCE 464 AA; 50134 MW; D5BD3083ACA39879 CRC64; MMLRAVFRRA SIRGSSSASG LGKSLQSSRV AVSAQFHSVS ATETLVPRGN HAHSFHHRSC PGCPDCSRTI INGYQGTALQ RWVRPFSSDS GDVVEAVVPH MGESITDGTL AAFLKKPGDR VEADEAIAQI ETDKVTIDIA SPASGVIQEF LVKEGDTVEP GNKVARISTS ADAVSHVAPS EKAPEKPAPK PSPPAEKPKV ESTKVAEKPK APSPPPPPPS KQSAKEPQLP PKDRERRVPM TRLRKRVATR LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFLEKHGVK LGLMSGFIKA AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRDADKMN FADIEKTING LAKKATEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP QSAILGMHSI VQRPMVVGGS VVPRPMMYVA LTYDHRLIDG REAVYFLRRI KDVVEDPQRL LLDI //