At5g55070

Functionⁱ

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).By similarity

Catalytic activityⁱ

Succinyl-CoA + enzyme N₆-(dihydrolipoyl)lysine = CoA + enzyme N₆-(S-succinyldihydrolipoyl)lysine.

Cofactorⁱ

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayⁱ: L-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:

Alpha-aminoadipic semialdehyde synthase (LKR/SDH)
Alpha-aminoadipic semialdehyde synthase (LKR/SDH)
no protein annotated in this organism
no protein annotated in this organism
no protein annotated in this organism
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial (At5g55070), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial (At4g26910)

This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	435	By similarity		1
Active siteⁱ	439	By similarity		1

GO - Molecular functionⁱ

dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
zinc ion binding
Source: TAIR
Inferred from direct assayⁱ
- 20018591

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
response to oxidative stress
Source: TAIR
Inferred from direct assayⁱ
- 12492832
tricarboxylic acid cycle Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Biological process	Tricarboxylic acid cycle

Enzyme and pathway databases

BioCycⁱ	ARA:AT5G55070-MONOMER
Reactomeⁱ	R-ATH-71064 Lysine catabolism R-ATH-71403 Citric acid cycle (TCA cycle)
UniPathwayⁱ	UPA00868;UER00840

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial (EC:2.3.1.61) Alternative name(s): 2-oxoglutarate dehydrogenase complex component E2-1 Short name: OGDC-E2-1 Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1 E2K-1
Gene namesⁱ	Ordered Locus Names:At5g55070 ORF Names:MCO15.2
Organismⁱ	Arabidopsis thaliana (Mouse-ear cress)
Taxonomic identifierⁱ	3702 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis
Proteomesⁱ	UP000006548 Componentⁱ: Chromosome 5

Organism-specific databases

Arabidopsis Information Portal More...Araportⁱ	AT5G55070
TAIRⁱ	locus:2161670 AT5G55070

Keywords - Cellular componentⁱ

Mitochondrion

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 86	Mitochondrion1 PublicationAdd BLAST		86
ChainⁱPRO_0000399512	87 – 464	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrialAdd BLAST		378

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	134	N6-lipoyllysinePROSITE-ProRule annotation		1

Proteomic databases

PaxDbⁱ	Q9FLQ4
PRIDEⁱ	Q9FLQ4

Expressionⁱ

Gene expression databases

ExpressionAtlasⁱ	Q9FLQ4 baseline and differential
Genevisibleⁱ	Q9FLQ4 AT

Interactionⁱ

Subunit structureⁱ

Forms a 24-polypeptide structural core with octahedral symmetry.By similarity

Protein-protein interaction databases

BioGridⁱ	20842, 4 interactors
IntActⁱ	Q9FLQ4, 1 interactor
STRINGⁱ	3702.AT5G55070.1

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q9FLQ4
SMRⁱ	Q9FLQ4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	93 – 168	Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST		76

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	179 – 231	Pro-richAdd BLAST		53

Sequence similaritiesⁱ

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domainⁱ

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0559 Eukaryota COG0508 LUCA
HOGENOMⁱ	HOG000281563
InParanoidⁱ	Q9FLQ4
KEGG Orthology (KO) More...KOⁱ	K00658
OMAⁱ	MKVPSPG
Database of Orthologous Groups More...OrthoDBⁱ	EOG09360CRB
PhylomeDBⁱ	Q9FLQ4

Family and domain databases

Gene3Dⁱ	3.30.559.10, 1 hit
InterProⁱ	View protein in InterPro IPR003016 2-oxoA_DH_lipoyl-BS IPR001078 2-oxoacid_DH_actylTfrase IPR000089 Biotin_lipoyl IPR023213 CAT-like_dom_sf IPR011053 Single_hybrid_motif IPR006255 SucB
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00198 2-oxoacid_dh, 1 hit PF00364 Biotin_lipoyl, 1 hit
SUPFAMⁱ	SSF51230 SSF51230, 1 hit
TIGRFAMsⁱ	TIGR01347 sucB, 1 hit
PROSITEⁱ	View protein in PROSITE PS50968 BIOTINYL_LIPOYL, 1 hit PS00189 LIPOYL, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q9FLQ4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MMLRAVFRRA SIRGSSSASG LGKSLQSSRV AVSAQFHSVS ATETLVPRGN 
        60         70         80         90        100
HAHSFHHRSC PGCPDCSRTI INGYQGTALQ RWVRPFSSDS GDVVEAVVPH 
       110        120        130        140        150
MGESITDGTL AAFLKKPGDR VEADEAIAQI ETDKVTIDIA SPASGVIQEF 
       160        170        180        190        200
LVKEGDTVEP GNKVARISTS ADAVSHVAPS EKAPEKPAPK PSPPAEKPKV 
       210        220        230        240        250
ESTKVAEKPK APSPPPPPPS KQSAKEPQLP PKDRERRVPM TRLRKRVATR 
       260        270        280        290        300
LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFLEKHGVK LGLMSGFIKA 
       310        320        330        340        350
AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRDADKMN 
       360        370        380        390        400
FADIEKTING LAKKATEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP 
       410        420        430        440        450
QSAILGMHSI VQRPMVVGGS VVPRPMMYVA LTYDHRLIDG REAVYFLRRI 
       460 
KDVVEDPQRL LLDI

Length:464

Mass (Da):50,134

Last modified:March 1, 2001 - v1

Checksum:ⁱD5BD3083ACA39879

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	30 – 34	VAVSA → LVASS in CAA11553 (Ref. 1) Curated	5
Sequence conflictⁱ	70	I → V in CAA11553 (Ref. 1) Curated	1
Sequence conflictⁱ	74	Y → F in CAA11553 (Ref. 1) Curated	1
Sequence conflictⁱ	218 – 219	Missing in CAA11553 (Ref. 1) Curated	2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AJ223803 mRNA Translation: CAA11553.1 AB010071 Genomic DNA Translation: BAB08576.1 CP002688 Genomic DNA Translation: AED96577.1 CP002688 Genomic DNA Translation: ANM68999.1 AY042897 mRNA Translation: AAK68837.1 AY128726 mRNA Translation: AAM91126.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001330709.1, NM_001345105.1 NP_200318.1, NM_124889.5
UniGeneⁱ	At.20476 At.71917

Genome annotation databases

EnsemblPlantsⁱ	AT5G55070.1; AT5G55070.1; AT5G55070 AT5G55070.2; AT5G55070.2; AT5G55070
GeneIDⁱ	835598
Grameneⁱ	AT5G55070.1; AT5G55070.1; AT5G55070 AT5G55070.2; AT5G55070.2; AT5G55070
KEGGⁱ	ath:AT5G55070

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9FLQ4	BnaA03g11590D protein		BRANA		535	UniRef90_Q9FLQ4
Uncharacterized protein (Fragment)		Brassica oleracea var. oleracea		513
Uncharacterized protein		BRARP		494
Uncharacterized protein		ARATH		466
2-oxoglutarate dehydrogenase E2 subunit		ARALL		463
+31

Protein	Similar proteins		Species	Score	Length	Source
Q9FLQ4	BnaA03g11590D protein		BRANA		535	UniRef50_Q9FLQ4
Uncharacterized protein (Fragment)		Brassica oleracea var. oleracea		513
Uncharacterized protein		BRARP		494
Uncharacterized protein		ARATH		466
2-oxoglutarate dehydrogenase E2 subunit		ARALL		463
+43

Entry informationⁱ

Entry nameⁱ	ODO2A_ARATH
Accessionⁱ	Q9FLQ4Primary (citable) accession number: Q9FLQ4 Secondary accession number(s): Q9ZRQ1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
	Last sequence update:	March 1, 2001
	Last modified:	April 25, 2018
	This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Plant Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9FLQ4 (ODO2A_ARATH)

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Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine degradation via saccharopine pathway

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Cytosol

Mitochondrion

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: L-lysine degradation via saccharopine pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ