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P19262

- ODO2_YEAST

UniProt

P19262 - ODO2_YEAST

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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: 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).

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei435 – 4351By similarity
Active sitei439 – 4391By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: SGD

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: SGD
  2. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  3. mitochondrial genome maintenance Source: SGD
  4. tricarboxylic acid cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciYEAST:YDR148C-MONOMER.
BRENDAi2.3.1.61. 984.
ReactomeiREACT_245486. Citric acid cycle (TCA cycle).
REACT_258556. Lysine catabolism.
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
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR148c.
SGDiS000002555. KGD2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial nucleoid Source: SGD
  2. mitochondrial oxoglutarate dehydrogenase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 463Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020478
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-lipoyllysinePROSITE-ProRule annotation
Modified residuei340 – 3401Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP19262.
PaxDbiP19262.
PeptideAtlasiP19262.
PRIDEiP19262.

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriP19262.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32202. 171 interactions.
DIPiDIP-1102N.
IntActiP19262. 27 interactions.
MINTiMINT-390263.
STRINGi4932.YDR148C.

Structurei

3D structure databases

ProteinModelPortaliP19262.
SMRiP19262. Positions 73-150, 233-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 14876Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati185 – 19061
Repeati191 – 19662
Repeati197 – 20263
Repeati204 – 20964; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 209254 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-[AV]Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Lipoyl, Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
GeneTreeiENSGT00760000119373.
HOGENOMiHOG000281563.
InParanoidiP19262.
KOiK00658.
OMAiIMPITIA.
OrthoDBiEOG73V6W0.

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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 20839PSQGV…EPKKA → HRKVSPQGKTQVRKRLQRKK LLQRKKPLQRKKLQNQKRT in AAA34720. (PubMed:2115121)CuratedAdd
BLAST
Sequence conflicti441 – 4455REAVT → EKLLS in AAA34720. (PubMed:2115121)Curated
Sequence conflicti460 – 4634MLLW → CCYGDLKFAAHTNLIS in AAA34720. (PubMed:2115121)Curated

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.

Cross-referencesi

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 .
PIRi S57975. XUBYSD.
RefSeqi NP_010432.3. NM_001180455.3.

3D structure databases

ProteinModelPortali P19262.
SMRi P19262. Positions 73-150, 233-462.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32202. 171 interactions.
DIPi DIP-1102N.
IntActi P19262. 27 interactions.
MINTi MINT-390263.
STRINGi 4932.YDR148C.

Proteomic databases

MaxQBi P19262.
PaxDbi P19262.
PeptideAtlasi P19262.
PRIDEi P19262.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR148C ; YDR148C ; YDR148C .
GeneIDi 851726.
KEGGi sce:YDR148C.

Organism-specific databases

CYGDi YDR148c.
SGDi S000002555. KGD2.

Phylogenomic databases

eggNOGi COG0508.
GeneTreei ENSGT00760000119373.
HOGENOMi HOG000281563.
InParanoidi P19262.
KOi K00658.
OMAi IMPITIA.
OrthoDBi EOG73V6W0.

Enzyme and pathway databases

UniPathwayi UPA00868 ; UER00840 .
BioCyci YEAST:YDR148C-MONOMER.
BRENDAi 2.3.1.61. 984.
Reactomei REACT_245486. Citric acid cycle (TCA cycle).
REACT_258556. Lysine catabolism.

Miscellaneous databases

NextBioi 969442.
PROi P19262.

Gene expression databases

Genevestigatori P19262.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01347. sucB. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiODO2_YEAST
AccessioniPrimary (citable) accession number: P19262
Secondary accession number(s): D6VSD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3