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Protein

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

Gene

KGD2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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).

Miscellaneous

Present with 7970 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

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. no protein annotated in this organism
  2. no protein annotated in this organism
  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, mitochondrial (KGD2)
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

GO - Biological processi

  • 2-oxoglutarate metabolic process Source: SGD
  • L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  • mitochondrial genome maintenance Source: SGD
  • tricarboxylic acid cycle Source: SGD

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyciYEAST:YDR148C-MONOMER
BRENDAi2.3.1.61 984
ReactomeiR-SCE-389661 Glyoxylate metabolism and glycine degradation
R-SCE-71064 Lysine catabolism
R-SCE-71403 Citric acid cycle (TCA cycle)
UniPathwayiUPA00868; UER00840

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
Gene namesi
Name:KGD2
Ordered Locus Names:YDR148C
ORF Names:YD8358.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR148C
SGDiS000002555 KGD2

Subcellular locationi

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000020478? – 463Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei114N6-lipoyllysinePROSITE-ProRule annotation1
Modified residuei340PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP19262
PaxDbiP19262
PRIDEiP19262

PTM databases

iPTMnetiP19262

Expressioni

Inductioni

Transcriptionally regulated by glucose and activated by the HAP2 and HAP3 proteins.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi32202354 interactors.
DIPiDIP-1102N
IntActiP19262 55 interactors.
MINTiP19262
STRINGi4932.YDR148C

Structurei

3D structure databases

ProteinModelPortaliP19262
SMRiP19262
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini73 – 148Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST76
Repeati185 – 19016
Repeati191 – 19626
Repeati197 – 20236
Repeati204 – 2094; approximate6

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni185 – 2094 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-[AV]Add BLAST25

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

GeneTreeiENSGT00890000139479
HOGENOMiHOG000281563
InParanoidiP19262
KOiK00658
OMAiMKVPSPG
OrthoDBiEOG092C3KQ8

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

Sequencei

Sequence statusi: Complete.

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

P19262-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSRATRTAA AKSLVKSKVA RNVMAASFVK RHASTSLFKQ ANKVESLGSI
60 70 80 90 100
YLSGKKISVA ANPFSITSNR FKSTSIEVPP MAESLTEGSL KEYTKNVGDF
110 120 130 140 150
IKEDELLATI ETDKIDIEVN SPVSGTVTKL NFKPEDTVTV GEELAQVEPG
160 170 180 190 200
EAPAEGSGES KPEPTEQAEP SQGVAARENS SEETASKKEA APKKEAAPKK
210 220 230 240 250
EVTEPKKADQ PKKTVSKAQE PPVASNSFTP FPRTETRVKM NRMRLRIAER
260 270 280 290 300
LKESQNTAAS LTTFNEVDMS ALMEMRKLYK DEIIKKTGTK FGFMGLFSKA
310 320 330 340 350
CTLAAKDIPA VNGAIEGDQI VYRDYTDISV AVATPKGLVT PVVRNAESLS
360 370 380 390 400
VLDIENEIVR LSHKARDGKL TLEDMTGGTF TISNGGVFGS LYGTPIINSP
410 420 430 440 450
QTAVLGLHGV KERPVTVNGQ IVSRPMMYLA LTYDHRLLDG REAVTFLKTV
460
KELIEDPRKM LLW
Length:463
Mass (Da):50,431
Last modified:February 1, 1996 - v2
Checksum:iC06FEB1DE385AE19
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti170 – 208PSQGV…EPKKA → HRKVSPQGKTQVRKRLQRKK LLQRKKPLQRKKLQNQKRT in AAA34720 (PubMed:2115121).CuratedAdd BLAST39
Sequence conflicti441 – 445REAVT → EKLLS in AAA34720 (PubMed:2115121).Curated5
Sequence conflicti460 – 463MLLW → CCYGDLKFAAHTNLIS in AAA34720 (PubMed:2115121).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34531 Genomic DNA Translation: AAA34720.1
Z50046 Genomic DNA Translation: CAA90371.1
BK006938 Genomic DNA Translation: DAA11991.1
PIRiS57975 XUBYSD
RefSeqiNP_010432.3, NM_001180455.3

Genome annotation databases

EnsemblFungiiYDR148C; YDR148C; YDR148C
GeneIDi851726
KEGGisce:YDR148C

Similar proteinsi

Entry informationi

Entry nameiODO2_YEAST
AccessioniPrimary (citable) accession number: P19262
Secondary accession number(s): D6VSD1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: March 28, 2018
This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome