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Q9FLQ4 (ODO2A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 Ref.5.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8686Mitochondrion Potential
Chain87 – 464378Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
PRO_0000399512

Regions

Domain94 – 16774Lipoyl-binding
Compositional bias179 – 23153Pro-rich

Sites

Active site4351 By similarity
Active site4391 By similarity

Amino acid modifications

Modified residue1341N6-lipoyllysine Potential

Experimental info

Sequence conflict30 – 345VAVSA → LVASS in CAA11553. Ref.1
Sequence conflict701I → V in CAA11553. Ref.1
Sequence conflict741Y → F in CAA11553. Ref.1
Sequence conflict218 – 2192Missing in CAA11553. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9FLQ4 [UniParc].

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

FASTA46450,134
        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' 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. expand/collapse author list , 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].
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: 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.
RefSeqNP_200318.1. NM_124889.4.
UniGeneAt.20476.
At.71917.

3D structure databases

ProteinModelPortalQ9FLQ4.
SMRQ9FLQ4. Positions 94-168, 235-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid20842. 4 interactions.
STRING3702.AT5G55070.1-P.

Proteomic databases

PaxDbQ9FLQ4.
PRIDEQ9FLQ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G55070.1; AT5G55070.1; AT5G55070.
GeneID835598.
KEGGath:AT5G55070.

Organism-specific databases

GeneFarm4414.
TAIRAT5G55070.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281563.
InParanoidQ9FLQ4.
KOK00658.
OMAMRMRIAQ.
PhylomeDBQ9FLQ4.

Enzyme and pathway databases

BioCycARA:AT5G55070-MONOMER.
UniPathwayUPA00868; UER00840.

Gene expression databases

GenevestigatorQ9FLQ4.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR003016. 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]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9FLQ4.

Entry information

Entry nameODO2A_ARATH
AccessionPrimary (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: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names