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Q8H107

- ODO2B_ARATH

UniProt

Q8H107 - ODO2B_ARATH

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Protein
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
Gene
At4g26910, F10M23.250
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 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. 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: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
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8585Mitochondrion Reviewed prediction
Add
BLAST
Chaini86 – 464379Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
PRO_0000399513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei133 – 1331N6-lipoyllysine Reviewed prediction

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.

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9999Missing in isoform 3.
VSP_039869Add
BLAST
Alternative sequencei62 – 621Missing in isoform 2.
VSP_039870

Sequence conflict

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

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 85 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

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