Q8H107 (ODO2B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
EC=2.3.1.61

Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2-2
Short name=OGDC-E2-2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2
E2K-2

Gene names

Ordered Locus Names:	At4g26910
ORF Names:	F10M23.250

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.
Sequence caution	The sequence AAM67267.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AY096643 differs from that shown. Reason: Frameshift at position 207. The sequence CAB36537.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79546.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Lipoyl Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	membrane Inferred from direct assay PubMed 17432890. Source: TAIR mitochondrion Inferred from direct assay Ref.6PubMed 15276431PubMed 18385124PubMed 22923678. Source: TAIR oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from direct assay PubMed 20018591. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8H107-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8H107-2)

The sequence of this isoform differs from the canonical sequence as follows:
     62-62: Missing.

Isoform 3 (identifier: Q8H107-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Note: May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 85	85	Mitochondrion Potential
	Chain	86 – 464	379	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial		PRO_0000399513
Regions
	Domain	93 – 166	74	Lipoyl-binding
	Compositional bias	217 – 220	4	Poly-Pro
Sites
	Active site	435	1	By similarity
	Active site	439	1	By similarity
Amino acid modifications
	Modified residue	133	1	N6-lipoyllysine Potential
Natural variations
	Alternative sequence	1 – 99	99	Missing in isoform 3.		VSP_039869
	Alternative sequence	62	1	Missing in isoform 2.		VSP_039870
Experimental info
	Sequence conflict	3	1	M → L in AAM67267. Ref.5
	Sequence conflict	21	1	A → G in AAM67267. Ref.5
	Sequence conflict	201	1	R → K in AAM67267. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: 6294B9767C967385	FASTA	464	50,059
	10 20 30 40 50 60 MMMRAVIRRA ASNGSSPSLF AKSLQSSRVA ASSPSLLSGS ETGAYLHRGN HAHSFHNLAL 70 80 90 100 110 120 PAGNSGISRS ASLVSSTLQR WVRPFSAETG DTVEAVVPHM GESITDGTLA TFLKKPGERV 130 140 150 160 170 180 QADEAIAQIE TDKVTIDIAS PASGVIQEFL VNEGDTVEPG TKVAIISKSE DTASQVTPSQ 190 200 210 220 230 240 KIPETTDTKP SPPAEDKQKP RVESAPVAEK PKAPSSPPPP KQSAKEPQLP PKERERRVPM 250 260 270 280 290 300 TRLRKRVATR LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFYEKHGVK LGLMSGFIKA 310 320 330 340 350 360 AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRGADKMN FAEIEKTINS 370 380 390 400 410 420 LAKKANEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP QSAILGMHSI VSRPMVVGGS 430 440 450 460 VVPRPMMYVA LTYDHRLIDG REAVYFLRRV KDVVEDPQRL LLDI
	Isoform 2 [UniParc]. Checksum: 2486A8763A9AE38E	FASTA	463	49,988
	10 20 30 40 50 60 MMMRAVIRRA ASNGSSPSLF AKSLQSSRVA ASSPSLLSGS ETGAYLHRGN HAHSFHNLAL 70 80 90 100 110 120 PGNSGISRSA SLVSSTLQRW VRPFSAETGD TVEAVVPHMG ESITDGTLAT FLKKPGERVQ 130 140 150 160 170 180 ADEAIAQIET DKVTIDIASP ASGVIQEFLV NEGDTVEPGT KVAIISKSED TASQVTPSQK 190 200 210 220 230 240 IPETTDTKPS PPAEDKQKPR VESAPVAEKP KAPSSPPPPK QSAKEPQLPP KERERRVPMT 250 260 270 280 290 300 RLRKRVATRL KDSQNTFALL TTFNEVDMTN LMKLRSQYKD AFYEKHGVKL GLMSGFIKAA 310 320 330 340 350 360 VSALQHQPVV NAVIDGDDII YRDYVDISIA VGTSKGLVVP VIRGADKMNF AEIEKTINSL 370 380 390 400 410 420 AKKANEGTIS IDEMAGGSFT VSNGGVYGSL ISTPIINPPQ SAILGMHSIV SRPMVVGGSV 430 440 450 460 VPRPMMYVAL TYDHRLIDGR EAVYFLRRVK DVVEDPQRLL LDI
	Isoform 3 [UniParc]. Checksum: 4903970E87280D29	FASTA	365	39,703
	10 20 30 40 50 60 MGESITDGTL ATFLKKPGER VQADEAIAQI ETDKVTIDIA SPASGVIQEF LVNEGDTVEP 70 80 90 100 110 120 GTKVAIISKS EDTASQVTPS QKIPETTDTK PSPPAEDKQK PRVESAPVAE KPKAPSSPPP 130 140 150 160 170 180 PKQSAKEPQL PPKERERRVP MTRLRKRVAT RLKDSQNTFA LLTTFNEVDM TNLMKLRSQY 190 200 210 220 230 240 KDAFYEKHGV KLGLMSGFIK AAVSALQHQP VVNAVIDGDD IIYRDYVDIS IAVGTSKGLV 250 260 270 280 290 300 VPVIRGADKM NFAEIEKTIN SLAKKANEGT ISIDEMAGGS FTVSNGGVYG SLISTPIINP 310 320 330 340 350 360 PQSAILGMHS IVSRPMVVGG SVVPRPMMYV ALTYDHRLID GREAVYFLRR VKDVVEDPQR LLLDI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Strain: cv. Columbia.
[4]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL035440 Genomic DNA. Translation: CAB36537.1. Sequence problems. AL161566 Genomic DNA. Translation: CAB79546.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE85267.1. CP002687 Genomic DNA. Translation: AEE85268.1. CP002687 Genomic DNA. Translation: AEE85269.1. AY096643 mRNA. No translation available. BT000926 mRNA. Translation: AAN41326.1. AK317635 mRNA. Translation: BAH20297.1. AY084248 mRNA. Translation: AAM67267.1. Different initiation.
IPI	IPI00518009. IPI00535095. IPI00540099.
PIR	T04814.
RefSeq	NP_567761.1. NM_118825.3. NP_849452.1. NM_179121.2. NP_849453.1. NM_179122.1.
UniGene	At.48904. At.71008.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ProteinModelPortal	Q8H107.
SMR	Q8H107. Positions 93-160, 235-464.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8H107. 1 interaction.
STRING	3702.AT4G26910.1-P.
Proteomic databases
PaxDb	Q8H107.
PRIDE	Q8H107.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G26910.1; AT4G26910.1; AT4G26910.
GeneID	828798.
KEGG	ath:AT4G26910.
Organism-specific databases
TAIR	At4g26910.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
InParanoid	Q8LGI7.
KO	K00658.
OMA	NANENNK.
PhylomeDB	Q8H107.
ProtClustDB	PLN02226.
Enzyme and pathway databases
UniPathway	UPA00868; UER00840.
Gene expression databases
Genevestigator	Q8H107.
Family and domain databases
Gene3D	3.30.559.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR011053. Single_hybrid_motif. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2B_ARATH

Accession

Primary (citable) accession number: Q8H107
Secondary accession number(s): Q3E9W2, Q8LGI7, Q9SZ31

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program