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P19262 (ODO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KGD2
Ordered Locus Names:YDR148C
ORF Names:YD8358.05C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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).

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently.

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.

Subcellular location

Mitochondrion.

Induction

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

Miscellaneous

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

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YMR31P199553EBI-12464,EBI-16295

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 463Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020478

Regions

Domain74 – 14774Lipoyl-binding
Repeat185 – 19061
Repeat191 – 19662
Repeat197 – 20263
Repeat204 – 20964; approximate
Region185 – 209254 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-[AV]

Sites

Active site4351 By similarity
Active site4391 By similarity

Amino acid modifications

Modified residue1141N6-lipoyllysine Potential
Modified residue3401Phosphothreonine Ref.5

Experimental info

Sequence conflict170 – 20839PSQGV…EPKKA → HRKVSPQGKTQVRKRLQRKK LLQRKKPLQRKKLQNQKRT in AAA34720. Ref.1
Sequence conflict441 – 4455REAVT → EKLLS in AAA34720. Ref.1
Sequence conflict460 – 4634MLLW → CCYGDLKFAAHTNLIS in AAA34720. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19262 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: C06FEB1DE385AE19

FASTA46350,431
        10         20         30         40         50         60 
MLSRATRTAA AKSLVKSKVA RNVMAASFVK RHASTSLFKQ ANKVESLGSI YLSGKKISVA 

        70         80         90        100        110        120 
ANPFSITSNR FKSTSIEVPP MAESLTEGSL KEYTKNVGDF IKEDELLATI ETDKIDIEVN 

       130        140        150        160        170        180 
SPVSGTVTKL NFKPEDTVTV GEELAQVEPG EAPAEGSGES KPEPTEQAEP SQGVAARENS 

       190        200        210        220        230        240 
SEETASKKEA APKKEAAPKK EVTEPKKADQ PKKTVSKAQE PPVASNSFTP FPRTETRVKM 

       250        260        270        280        290        300 
NRMRLRIAER LKESQNTAAS LTTFNEVDMS ALMEMRKLYK DEIIKKTGTK FGFMGLFSKA 

       310        320        330        340        350        360 
CTLAAKDIPA VNGAIEGDQI VYRDYTDISV AVATPKGLVT PVVRNAESLS VLDIENEIVR 

       370        380        390        400        410        420 
LSHKARDGKL TLEDMTGGTF TISNGGVFGS LYGTPIINSP QTAVLGLHGV KERPVTVNGQ 

       430        440        450        460 
IVSRPMMYLA LTYDHRLLDG REAVTFLKTV KELIEDPRKM LLW

« Hide

References

« Hide 'large scale' references
[1]"Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase."
Repetto B., Tzagoloff A.
Mol. Cell. Biol. 10:4221-4232(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S288c / FY1678.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, MASS SPECTROMETRY.
Strain: ATCC 76625 / YPH499.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34531 Genomic DNA. Translation: AAA34720.1.
Z50046 Genomic DNA. Translation: CAA90371.1.
BK006938 Genomic DNA. Translation: DAA11991.1.
PIRXUBYSD. S57975.
RefSeqNP_010432.3. NM_001180455.3.

3D structure databases

ProteinModelPortalP19262.
SMRP19262. Positions 73-150, 233-462.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1102N.
IntActP19262. 29 interactions.
MINTMINT-390263.
STRING4932.YDR148C.

Proteomic databases

PaxDbP19262.
PeptideAtlasP19262.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR148C; YDR148C; YDR148C.
GeneID851726.
KEGGsce:YDR148C.

Organism-specific databases

CYGDYDR148c.
SGDS000002555. KGD2.

Phylogenomic databases

eggNOGCOG0508.
GeneTreeENSGT00560000077303.
HOGENOMHOG000281563.
KOK00658.
OMAVNADNEI.
OrthoDBEOG483HD4.

Enzyme and pathway databases

BioCycYEAST:YDR148C-MONOMER.
BRENDA2.3.1.61. 984.
UniPathwayUPA00868; UER00840.

Gene expression databases

GenevestigatorP19262.
GermOnlineYDR148C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
InterProIPR003016. 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]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMSSF51230. Hybrid_motif. 1 hit.
TIGRFAMsTIGR01347. sucB. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969442.

Entry information

Entry nameODO2_YEAST
AccessionPrimary (citable) accession number: P19262
Secondary accession number(s): D6VSD1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: May 29, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents