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 17-JUN-2020, entry version 126. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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 PubMed=9628582; DOI=10.1093/dnares/5.1.41; RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence RT features of the regions of 1,456,315 bp covered by nineteen physically RT assigned P1 and TAC clones."; RL DNA Res. 5:41-54(1998). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP 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 highlights RT signaling and regulatory components, provides assessment of targeting RT prediction programs, and indicates plant-specific mitochondrial proteins."; RL Plant Cell 16:241-256(2004). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER RP PHE-86. RX PubMed=25732537; DOI=10.1093/jxb/erv064; RA Carrie C., Venne A.S., Zahedi R.P., Soll J.; RT "Identification of cleavage sites and substrate proteins for two RT mitochondrial intermediate peptidases in Arabidopsis thaliana."; RL J. Exp. Bot. 66:2691-2708(2015). 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-oxoglutarate CC dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase CC complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)- CC succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex CC component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, CC Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250}; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine CC pathway; glutaryl-CoA from L-lysine: step 6/6. CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022, CC ECO:0000305|PubMed:25732537}. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000305}. 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; CP002688; AED96577.1; -; Genomic_DNA. DR EMBL; CP002688; ANM68999.1; -; Genomic_DNA. DR EMBL; AY042897; AAK68837.1; -; mRNA. DR EMBL; AY128726; AAM91126.1; -; mRNA. DR RefSeq; NP_001330709.1; NM_001345105.1. DR RefSeq; NP_200318.1; NM_124889.5. DR SMR; Q9FLQ4; -. DR BioGRID; 20842; 11. DR IntAct; Q9FLQ4; 1. DR STRING; 3702.AT5G55070.1; -. DR MetOSite; Q9FLQ4; -. DR PaxDb; Q9FLQ4; -. DR PRIDE; Q9FLQ4; -. DR ProteomicsDB; 250874; -. DR EnsemblPlants; AT5G55070.1; AT5G55070.1; AT5G55070. DR EnsemblPlants; AT5G55070.2; AT5G55070.2; AT5G55070. DR GeneID; 835598; -. DR Gramene; AT5G55070.1; AT5G55070.1; AT5G55070. DR Gramene; AT5G55070.2; AT5G55070.2; AT5G55070. DR KEGG; ath:AT5G55070; -. DR Araport; AT5G55070; -. DR TAIR; locus:2161670; AT5G55070. DR eggNOG; KOG0559; Eukaryota. DR eggNOG; COG0508; LUCA. DR HOGENOM; CLU_016733_0_2_1; -. DR InParanoid; Q9FLQ4; -. DR KO; K00658; -. DR OMA; DMAGATF; -. DR OrthoDB; 850255at2759; -. DR PhylomeDB; Q9FLQ4; -. DR BioCyc; ARA:AT5G55070-MONOMER; -. DR UniPathway; UPA00868; UER00840. DR PRO; PR:Q9FLQ4; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; Q9FLQ4; baseline and differential. DR Genevisible; Q9FLQ4; AT. 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:0009536; C:plastid; HDA:TAIR. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008270; F:zinc ion binding; IDA:TAIR. DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. DR GO; GO:0006979; P:response to oxidative stress; IDA:TAIR. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 1. 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_sf. DR InterPro; IPR011053; Single_hybrid_motif. DR InterPro; IPR006255; SucB. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR SUPFAM; SSF51230; SSF51230; 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; Lipoyl; Mitochondrion; Reference proteome; Transferase; KW Transit peptide; Tricarboxylic acid cycle. FT TRANSIT 1..86 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:25732537" FT CHAIN 87..464 FT /note="Dihydrolipoyllysine-residue succinyltransferase FT component of 2-oxoglutarate dehydrogenase complex 1, FT mitochondrial" FT /id="PRO_0000399512" FT DOMAIN 93..168 FT /note="Lipoyl-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT COMPBIAS 179..231 FT /note="Pro-rich" FT ACT_SITE 435 FT /evidence="ECO:0000250" FT ACT_SITE 439 FT /evidence="ECO:0000250" FT MOD_RES 134 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT CONFLICT 30..34 FT /note="VAVSA -> LVASS (in Ref. 1; CAA11553)" FT /evidence="ECO:0000305" FT CONFLICT 70 FT /note="I -> V (in Ref. 1; CAA11553)" FT /evidence="ECO:0000305" FT CONFLICT 74 FT /note="Y -> F (in Ref. 1; CAA11553)" FT /evidence="ECO:0000305" FT CONFLICT 218..219 FT /note="Missing (in Ref. 1; CAA11553)" FT /evidence="ECO:0000305" 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 //