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

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Q9FLQ4 (ODO2A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Ordered Locus Names:	At5g55070
ORF Names:	MCO15.2

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › 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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
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 response to oxidative stress Inferred from direct assay PubMed 12492832. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosolic ribosome Inferred from direct assay PubMed 15821981. Source: TAIR mitochondrion Inferred from direct assay PubMed 12492832 Ref.5 PubMed 14764908 PubMed 15276431 PubMed 18385124 PubMed 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 86

Mitochondrion Potential

Chain

87 – 464

378

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

PRO_0000399512

Regions

Domain

94 – 167

Lipoyl-binding

Compositional bias

179 – 231

Pro-rich

Sites

Active site

435

By similarity

Active site

439

By similarity

Amino acid modifications

Modified residue

134

N6-lipoyllysine Potential

Experimental info

Sequence conflict

30 – 34

VAVSA → LVASS in CAA11553. Ref.1

Sequence conflict

I → V in CAA11553. Ref.1

Sequence conflict

Y → F in CAA11553. Ref.1

Sequence conflict

218 – 219

Missing in CAA11553. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FLQ4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D5BD3083ACA39879
Show »

FASTA

464

50,134

        10         20         30         40         50         60 
MMLRAVFRRA SIRGSSSASG LGKSLQSSRV AVSAQFHSVS ATETLVPRGN HAHSFHHRSC 

        70         80         90        100        110        120 
PGCPDCSRTI INGYQGTALQ RWVRPFSSDS GDVVEAVVPH MGESITDGTL AAFLKKPGDR 

       130        140        150        160        170        180 
VEADEAIAQI ETDKVTIDIA SPASGVIQEF LVKEGDTVEP GNKVARISTS ADAVSHVAPS 

       190        200        210        220        230        240 
EKAPEKPAPK PSPPAEKPKV ESTKVAEKPK APSPPPPPPS KQSAKEPQLP PKDRERRVPM 

       250        260        270        280        290        300 
TRLRKRVATR LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFLEKHGVK LGLMSGFIKA 

       310        320        330        340        350        360 
AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRDADKMN FADIEKTING 

       370        380        390        400        410        420 
LAKKATEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP QSAILGMHSI VQRPMVVGGS 

       430        440        450        460 
VVPRPMMYVA LTYDHRLIDG REAVYFLRRI KDVVEDPQRL LLDI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of 2-oxoglutarate dehydrogenase from Arabidopsis thaliana." Machuy N., Klein M., Mueller-Roeber B. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones." Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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	AJ223803 mRNA. Translation: CAA11553.1. AB010071 Genomic DNA. Translation: BAB08576.1. CP002688 Genomic DNA. Translation: AED96577.1. AY042897 mRNA. Translation: AAK68837.1. AY128726 mRNA. Translation: AAM91126.1.
IPI	IPI00531713.
RefSeq	NP_200318.1. NM_124889.4.
UniGene	At.20476. At.71917.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ProteinModelPortal	Q9FLQ4.
SMR	Q9FLQ4. Positions 94-168, 235-464.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G55070.1-P.
Proteomic databases
PaxDb	Q9FLQ4.
PRIDE	Q9FLQ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G55070.1; AT5G55070.1; AT5G55070.
GeneID	835598.
KEGG	ath:AT5G55070.
Organism-specific databases
GeneFarm	4414.
TAIR	At5g55070.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
InParanoid	Q9FLQ4.
KO	K00658.
OMA	IINMPQT.
PhylomeDB	Q9FLQ4.
ProtClustDB	PLN02226.
Enzyme and pathway databases
UniPathway	UPA00868; UER00840.
Gene expression databases
Genevestigator	Q9FLQ4.
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

ODO2A_ARATH

Accession

Primary (citable) accession number: Q9FLQ4
Secondary accession number(s): Q9ZRQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents