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Q8H107

- ODO2B_ARATH

UniProt

Q8H107 - ODO2B_ARATH

Protein

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

Gene

At4g26910

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 86 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      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. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciARA:AT4G26910-MONOMER.
    ARA:GQT-1019-MONOMER.
    ARA:GQT-1020-MONOMER.
    UniPathwayiUPA00868; UER00840.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial (EC:2.3.1.61)
    Alternative name(s):
    2-oxoglutarate dehydrogenase complex component E2-2
    Short name:
    OGDC-E2-2
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2
    E2K-2
    Gene namesi
    Ordered Locus Names:At4g26910
    ORF Names:F10M23.250
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G26910.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. membrane 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 – 8585MitochondrionSequence AnalysisAdd
    BLAST
    Chaini86 – 464379Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrialPRO_0000399513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei133 – 1331N6-lipoyllysineSequence Analysis

    Proteomic databases

    PaxDbiQ8H107.
    PRIDEiQ8H107.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8H107.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi14085. 1 interaction.
    IntActiQ8H107. 1 interaction.
    STRINGi3702.AT4G26910.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8H107.
    SMRiQ8H107. Positions 93-160, 235-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 16674Lipoyl-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi217 – 2204Poly-Pro

    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.
    InParanoidiQ8LGI7.
    KOiK00658.
    OMAiIMPITIA.
    PhylomeDBiQ8H107.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8H107-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMMRAVIRRA ASNGSSPSLF AKSLQSSRVA ASSPSLLSGS ETGAYLHRGN    50
    HAHSFHNLAL PAGNSGISRS ASLVSSTLQR WVRPFSAETG DTVEAVVPHM 100
    GESITDGTLA TFLKKPGERV QADEAIAQIE TDKVTIDIAS PASGVIQEFL 150
    VNEGDTVEPG TKVAIISKSE DTASQVTPSQ KIPETTDTKP SPPAEDKQKP 200
    RVESAPVAEK PKAPSSPPPP KQSAKEPQLP PKERERRVPM TRLRKRVATR 250
    LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFYEKHGVK LGLMSGFIKA 300
    AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRGADKMN 350
    FAEIEKTINS LAKKANEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP 400
    QSAILGMHSI VSRPMVVGGS VVPRPMMYVA LTYDHRLIDG REAVYFLRRV 450
    KDVVEDPQRL LLDI 464
    Length:464
    Mass (Da):50,059
    Last modified:October 5, 2010 - v2
    Checksum:i6294B9767C967385
    GO
    Isoform 2 (identifier: Q8H107-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         62-62: Missing.

    Show »
    Length:463
    Mass (Da):49,988
    Checksum:i2486A8763A9AE38E
    GO
    Isoform 3 (identifier: Q8H107-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-99: Missing.

    Note: May be due to an intron retention. No experimental confirmation available.

    Show »
    Length:365
    Mass (Da):39,703
    Checksum:i4903970E87280D29
    GO

    Sequence cautioni

    The sequence AY096643 differs from that shown. Reason: Frameshift at position 207.
    The sequence AAM67267.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB36537.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB79546.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31M → L in AAM67267. 1 PublicationCurated
    Sequence conflicti21 – 211A → G in AAM67267. 1 PublicationCurated
    Sequence conflicti201 – 2011R → K in AAM67267. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9999Missing in isoform 3. 1 PublicationVSP_039869Add
    BLAST
    Alternative sequencei62 – 621Missing in isoform 2. 2 PublicationsVSP_039870

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035440 Genomic DNA. Translation: CAB36537.1. Sequence problems.
    AL161566 Genomic DNA. Translation: CAB79546.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85267.1.
    CP002687 Genomic DNA. Translation: AEE85268.1.
    CP002687 Genomic DNA. Translation: AEE85269.1.
    AY096643 mRNA. No translation available.
    BT000926 mRNA. Translation: AAN41326.1.
    AK317635 mRNA. Translation: BAH20297.1.
    AY084248 mRNA. Translation: AAM67267.1. Different initiation.
    PIRiT04814.
    RefSeqiNP_567761.1. NM_118825.3. [Q8H107-1]
    NP_849452.1. NM_179121.2. [Q8H107-2]
    NP_849453.1. NM_179122.1. [Q8H107-3]
    UniGeneiAt.48904.
    At.71008.

    Genome annotation databases

    EnsemblPlantsiAT4G26910.1; AT4G26910.1; AT4G26910. [Q8H107-1]
    GeneIDi828798.
    KEGGiath:AT4G26910.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL035440 Genomic DNA. Translation: CAB36537.1 . Sequence problems.
    AL161566 Genomic DNA. Translation: CAB79546.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE85267.1 .
    CP002687 Genomic DNA. Translation: AEE85268.1 .
    CP002687 Genomic DNA. Translation: AEE85269.1 .
    AY096643 mRNA. No translation available.
    BT000926 mRNA. Translation: AAN41326.1 .
    AK317635 mRNA. Translation: BAH20297.1 .
    AY084248 mRNA. Translation: AAM67267.1 . Different initiation.
    PIRi T04814.
    RefSeqi NP_567761.1. NM_118825.3. [Q8H107-1 ]
    NP_849452.1. NM_179121.2. [Q8H107-2 ]
    NP_849453.1. NM_179122.1. [Q8H107-3 ]
    UniGenei At.48904.
    At.71008.

    3D structure databases

    ProteinModelPortali Q8H107.
    SMRi Q8H107. Positions 93-160, 235-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14085. 1 interaction.
    IntActi Q8H107. 1 interaction.
    STRINGi 3702.AT4G26910.1-P.

    Proteomic databases

    PaxDbi Q8H107.
    PRIDEi Q8H107.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G26910.1 ; AT4G26910.1 ; AT4G26910 . [Q8H107-1 ]
    GeneIDi 828798.
    KEGGi ath:AT4G26910.

    Organism-specific databases

    TAIRi AT4G26910.

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281563.
    InParanoidi Q8LGI7.
    KOi K00658.
    OMAi IMPITIA.
    PhylomeDBi Q8H107.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00840 .
    BioCyci ARA:AT4G26910-MONOMER.
    ARA:GQT-1019-MONOMER.
    ARA:GQT-1020-MONOMER.

    Miscellaneous databases

    PROi Q8H107.

    Gene expression databases

    Genevestigatori Q8H107.

    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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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] (ISOFORMS 2 AND 3).
      Strain: cv. Columbia.
    4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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 nameiODO2B_ARATH
    AccessioniPrimary (citable) accession number: Q8H107
    Secondary accession number(s): Q3E9W2, Q8LGI7, Q9SZ31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 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