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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: 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).

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

GO - Cellular componenti

  • mitochondrial nucleoid Source: SGD
  • mitochondrial oxoglutarate dehydrogenase complex Source: SGD

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.
PRIDEiP19262.

PTM databases

iPTMnetiP19262.

Expressioni

Inductioni

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

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
YMR31P199553EBI-12464,EBI-16295

Protein-protein interaction databases

BioGridi32202. 353 interactors.
DIPiDIP-1102N.
IntActiP19262. 28 interactors.
MINTiMINT-390263.
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

GeneTreeiENSGT00880000137953.
HOGENOMiHOG000281563.
InParanoidiP19262.
KOiK00658.
OMAiMKVPSPG.
OrthoDBiEOG092C3KQ8.

Family and domain databases

InterProiView protein in InterPro
IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR000089. Biotin_lipoyl.
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

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.

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: July 5, 2017
This is version 173 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names