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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: -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

Caution

Catalytic activityi

Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic 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

AraportiAT4G26910
TAIRilocus:2116432 AT4G26910

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 85Mitochondrion1 PublicationAdd 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

ExpressionAtlasiQ8H107 baseline and differential
GenevisibleiQ8H107 AT

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi140851 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

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0559 Eukaryota
COG0508 LUCA
HOGENOMiHOG000281563
InParanoidiQ8H107
KOiK00658
OMAiGMHAIFQ
OrthoDBiEOG09360CRB
PhylomeDBiQ8H107

Family and domain databases

Gene3Di3.30.559.101 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR011053 Single_hybrid_motif
IPR006255 SucB
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
TIGRFAMsiTIGR01347 sucB, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit

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]
AT4G26910.2; AT4G26910.2; AT4G26910 [Q8H107-2]
AT4G26910.3; AT4G26910.3; AT4G26910 [Q8H107-3]
GeneIDi828798
GrameneiAT4G26910.1; AT4G26910.1; AT4G26910 [Q8H107-1]
AT4G26910.2; AT4G26910.2; AT4G26910 [Q8H107-2]
AT4G26910.3; AT4G26910.3; AT4G26910 [Q8H107-3]
KEGGiath:AT4G26910

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiODO2B_ARATH
AccessioniPrimary (citable) accession number: Q8H107
Secondary accession number(s): Q3E9W2, Q8LGI7, Q9SZ31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: April 25, 2018
This is version 108 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome