ODO2B_ARATH
ID ODO2B_ARATH Reviewed; 464 AA.
AC Q8H107; Q3E9W2; Q8LGI7; Q9SZ31;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial;
DE EC=2.3.1.61;
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2-2;
DE Short=OGDC-E2-2;
DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2;
DE AltName: Full=E2K-2;
DE Flags: Precursor;
GN OrderedLocusNames=At4g26910; ORFNames=F10M23.250;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-85.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8H107-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H107-2; Sequence=VSP_039870;
CC Name=3;
CC IsoId=Q8H107-3; Sequence=VSP_039869;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM67267.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AY096643; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB36537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035440; CAB36537.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161566; CAB79546.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85267.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85268.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85269.1; -; Genomic_DNA.
DR EMBL; AY096643; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT000926; AAN41326.1; -; mRNA.
DR EMBL; AK317635; BAH20297.1; -; mRNA.
DR EMBL; AY084248; AAM67267.1; ALT_INIT; mRNA.
DR PIR; T04814; T04814.
DR RefSeq; NP_567761.1; NM_118825.3. [Q8H107-1]
DR RefSeq; NP_849452.1; NM_179121.3. [Q8H107-2]
DR RefSeq; NP_849453.1; NM_179122.1. [Q8H107-3]
DR AlphaFoldDB; Q8H107; -.
DR SMR; Q8H107; -.
DR BioGRID; 14085; 23.
DR IntAct; Q8H107; 1.
DR STRING; 3702.AT4G26910.1; -.
DR PaxDb; Q8H107; -.
DR PRIDE; Q8H107; -.
DR ProteomicsDB; 250875; -. [Q8H107-1]
DR EnsemblPlants; AT4G26910.1; AT4G26910.1; AT4G26910. [Q8H107-1]
DR EnsemblPlants; AT4G26910.2; AT4G26910.2; AT4G26910. [Q8H107-2]
DR EnsemblPlants; AT4G26910.3; AT4G26910.3; AT4G26910. [Q8H107-3]
DR GeneID; 828798; -.
DR Gramene; AT4G26910.1; AT4G26910.1; AT4G26910. [Q8H107-1]
DR Gramene; AT4G26910.2; AT4G26910.2; AT4G26910. [Q8H107-2]
DR Gramene; AT4G26910.3; AT4G26910.3; AT4G26910. [Q8H107-3]
DR KEGG; ath:AT4G26910; -.
DR Araport; AT4G26910; -.
DR TAIR; locus:2116432; AT4G26910.
DR eggNOG; KOG0559; Eukaryota.
DR InParanoid; Q8H107; -.
DR OMA; MKVPSPG; -.
DR OrthoDB; 850255at2759; -.
DR PhylomeDB; Q8H107; -.
DR BioCyc; ARA:AT4G26910-MON; -.
DR UniPathway; UPA00868; UER00840.
DR PRO; PR:Q8H107; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H107; baseline and differential.
DR Genevisible; Q8H107; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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; Alternative splicing; Lipoyl; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..85
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 86..464
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex 2,
FT mitochondrial"
FT /id="PRO_0000399513"
FT DOMAIN 92..167
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 167..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /evidence="ECO:0000250"
FT MOD_RES 133
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039869"
FT VAR_SEQ 62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19423640"
FT /id="VSP_039870"
FT CONFLICT 3
FT /note="M -> L (in Ref. 5; AAM67267)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="A -> G (in Ref. 5; AAM67267)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="R -> K (in Ref. 5; AAM67267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 50059 MW; 6294B9767C967385 CRC64;
MMMRAVIRRA ASNGSSPSLF AKSLQSSRVA ASSPSLLSGS ETGAYLHRGN HAHSFHNLAL
PAGNSGISRS ASLVSSTLQR WVRPFSAETG DTVEAVVPHM GESITDGTLA TFLKKPGERV
QADEAIAQIE TDKVTIDIAS PASGVIQEFL VNEGDTVEPG TKVAIISKSE DTASQVTPSQ
KIPETTDTKP SPPAEDKQKP RVESAPVAEK PKAPSSPPPP KQSAKEPQLP PKERERRVPM
TRLRKRVATR LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFYEKHGVK LGLMSGFIKA
AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRGADKMN FAEIEKTINS
LAKKANEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP QSAILGMHSI VSRPMVVGGS
VVPRPMMYVA LTYDHRLIDG REAVYFLRRV KDVVEDPQRL LLDI
