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Q9FLQ4

- ODO2A_ARATH

UniProt

Q9FLQ4 - ODO2A_ARATH

Protein

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

Gene

At5g55070

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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 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 – 4351By similarity
    Active sitei439 – 4391By 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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8686MitochondrionSequence AnalysisAdd
    BLAST
    Chaini87 – 464378Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrialPRO_0000399512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei134 – 1341N6-lipoyllysineSequence Analysis

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    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

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    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 94 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