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Protein

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

Gene

At4g26910

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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).By similarity

Catalytic activityi

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

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Pathwayi: L-lysine degradation via saccharopine pathway

This protein is involved in step 6 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Alpha-aminoadipic semialdehyde synthase (LKR/SDH)
  2. Alpha-aminoadipic semialdehyde synthase (LKR/SDH)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial (At4g26910), Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial (At5g55070)
This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei435By similarity1
Active sitei439By similarity1

GO - Molecular functioni

  • dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
  • zinc ion binding Source: TAIR

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:AT4G26910-MONOMER.
ReactomeiR-ATH-71064. Lysine catabolism.
R-ATH-71403. Citric acid cycle (TCA cycle).
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
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G26910.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: TAIR
  • mitochondrion Source: TAIR
  • oxoglutarate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 85MitochondrionSequence analysisAdd BLAST85
ChainiPRO_000039951386 – 464Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrialAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei133N6-lipoyllysinePROSITE-ProRule annotation1

Proteomic databases

PaxDbiQ8H107.
PRIDEiQ8H107.

Expressioni

Gene expression databases

GenevisibleiQ8H107. AT.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi14085. 1 interactor.
IntActiQ8H107. 1 interactor.
STRINGi3702.AT4G26910.1.

Structurei

3D structure databases

ProteinModelPortaliQ8H107.
SMRiQ8H107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini92 – 167Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi217 – 220Poly-Pro4

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
HOGENOMiHOG000281563.
InParanoidiQ8H107.
KOiK00658.
OMAiRPASCIP.
OrthoDBiEOG09360CRB.
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. AlignAdd to basket

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

        10         20         30         40         50
MMMRAVIRRA ASNGSSPSLF AKSLQSSRVA ASSPSLLSGS ETGAYLHRGN
60 70 80 90 100
HAHSFHNLAL PAGNSGISRS ASLVSSTLQR WVRPFSAETG DTVEAVVPHM
110 120 130 140 150
GESITDGTLA TFLKKPGERV QADEAIAQIE TDKVTIDIAS PASGVIQEFL
160 170 180 190 200
VNEGDTVEPG TKVAIISKSE DTASQVTPSQ KIPETTDTKP SPPAEDKQKP
210 220 230 240 250
RVESAPVAEK PKAPSSPPPP KQSAKEPQLP PKERERRVPM TRLRKRVATR
260 270 280 290 300
LKDSQNTFAL LTTFNEVDMT NLMKLRSQYK DAFYEKHGVK LGLMSGFIKA
310 320 330 340 350
AVSALQHQPV VNAVIDGDDI IYRDYVDISI AVGTSKGLVV PVIRGADKMN
360 370 380 390 400
FAEIEKTINS LAKKANEGTI SIDEMAGGSF TVSNGGVYGS LISTPIINPP
410 420 430 440 450
QSAILGMHSI VSRPMVVGGS VVPRPMMYVA LTYDHRLIDG REAVYFLRRV
460
KDVVEDPQRL LLDI
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 AAM67267 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AY096643 differs from that shown. Reason: Frameshift at position 207.Curated
The sequence CAB36537 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB79546 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3M → L in AAM67267 (Ref. 5) Curated1
Sequence conflicti21A → G in AAM67267 (Ref. 5) Curated1
Sequence conflicti201R → K in AAM67267 (Ref. 5) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0398691 – 99Missing in isoform 3. 1 PublicationAdd BLAST99
Alternative sequenceiVSP_03987062Missing in isoform 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_179121.3. [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.
GrameneiAT4G26910.1; AT4G26910.1; AT4G26910.
KEGGiath:AT4G26910.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_179121.3. [Q8H107-2]
NP_849453.1. NM_179122.1. [Q8H107-3]
UniGeneiAt.48904.
At.71008.

3D structure databases

ProteinModelPortaliQ8H107.
SMRiQ8H107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14085. 1 interactor.
IntActiQ8H107. 1 interactor.
STRINGi3702.AT4G26910.1.

Proteomic databases

PaxDbiQ8H107.
PRIDEiQ8H107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G26910.1; AT4G26910.1; AT4G26910. [Q8H107-1]
GeneIDi828798.
GrameneiAT4G26910.1; AT4G26910.1; AT4G26910.
KEGGiath:AT4G26910.

Organism-specific databases

TAIRiAT4G26910.

Phylogenomic databases

eggNOGiKOG0559. Eukaryota.
COG0508. LUCA.
HOGENOMiHOG000281563.
InParanoidiQ8H107.
KOiK00658.
OMAiRPASCIP.
OrthoDBiEOG09360CRB.
PhylomeDBiQ8H107.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
BioCyciARA:AT4G26910-MONOMER.
ReactomeiR-ATH-71064. Lysine catabolism.
R-ATH-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiQ8H107.

Gene expression databases

GenevisibleiQ8H107. AT.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.