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Q9FLQ4

- ODO2A_ARATH

UniProt

Q9FLQ4 - ODO2A_ARATH

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Protein
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
Gene
At5g55070, MCO15.2
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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.

Catalytic activityi

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei435 – 4351 By similarity
Active sitei439 – 4391 By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
  2. zinc ion binding Source: TAIR

GO - Biological processi

  1. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  2. response to oxidative stress Source: TAIR
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:AT5G55070-MONOMER.
UniPathwayiUPA00868; 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
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G55070.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. cytosolic ribosome Source: TAIR
  2. mitochondrion Source: TAIR
  3. oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8686Mitochondrion Reviewed prediction
Add
BLAST
Chaini87 – 464378Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
PRO_0000399512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei134 – 1341N6-lipoyllysine Reviewed prediction

Proteomic databases

PaxDbiQ9FLQ4.
PRIDEiQ9FLQ4.

Expressioni

Gene expression databases

GenevestigatoriQ9FLQ4.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi20842. 4 interactions.
IntActiQ9FLQ4. 1 interaction.
STRINGi3702.AT5G55070.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9FLQ4.
SMRiQ9FLQ4. Positions 94-168, 235-464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini94 – 16774Lipoyl-binding
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi179 – 23153Pro-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
InParanoidiQ9FLQ4.
KOiK00658.
OMAiMRMRIAQ.
PhylomeDBiQ9FLQ4.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9FLQ4-1 [UniParc]FASTAAdd to Basket

« Hide

MMLRAVFRRA SIRGSSSASG LGKSLQSSRV AVSAQFHSVS ATETLVPRGN    50
HAHSFHHRSC PGCPDCSRTI INGYQGTALQ RWVRPFSSDS GDVVEAVVPH 100
MGESITDGTL AAFLKKPGDR VEADEAIAQI ETDKVTIDIA SPASGVIQEF 150
LVKEGDTVEP GNKVARISTS ADAVSHVAPS EKAPEKPAPK PSPPAEKPKV 200
ESTKVAEKPK APSPPPPPPS KQSAKEPQLP PKDRERRVPM TRLRKRVATR 250
LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFLEKHGVK LGLMSGFIKA 300
AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRDADKMN 350
FADIEKTING LAKKATEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP 400
QSAILGMHSI VQRPMVVGGS VVPRPMMYVA LTYDHRLIDG REAVYFLRRI 450
KDVVEDPQRL LLDI 464
Length:464
Mass (Da):50,134
Last modified:March 1, 2001 - v1
Checksum:iD5BD3083ACA39879
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 345VAVSA → LVASS in CAA11553. 1 Publication
Sequence conflicti70 – 701I → V in CAA11553. 1 Publication
Sequence conflicti74 – 741Y → F in CAA11553. 1 Publication
Sequence conflicti218 – 2192Missing in CAA11553. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_200318.1. NM_124889.4.
UniGeneiAt.20476.
At.71917.

Genome annotation databases

EnsemblPlantsiAT5G55070.1; AT5G55070.1; AT5G55070.
GeneIDi835598.
KEGGiath:AT5G55070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_200318.1. NM_124889.4.
UniGenei At.20476.
At.71917.

3D structure databases

ProteinModelPortali Q9FLQ4.
SMRi Q9FLQ4. Positions 94-168, 235-464.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 20842. 4 interactions.
IntActi Q9FLQ4. 1 interaction.
STRINGi 3702.AT5G55070.1-P.

Proteomic databases

PaxDbi Q9FLQ4.
PRIDEi Q9FLQ4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

GeneFarmi 4414.
TAIRi AT5G55070.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281563.
InParanoidi Q9FLQ4.
KOi K00658.
OMAi MRMRIAQ.
PhylomeDBi Q9FLQ4.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
BioCyci ARA:AT5G55070-MONOMER.

Miscellaneous databases

PROi Q9FLQ4.

Gene expression databases

Genevestigatori Q9FLQ4.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
InterProi 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01347. sucB. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiODO2A_ARATH
AccessioniPrimary (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: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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