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P20967 (ODO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoglutarate dehydrogenase, mitochondrial

EC=1.2.4.2
Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1
Short name=OGDC-E1
Alpha-ketoglutarate dehydrogenase
Gene names
Name:KGD1
Synonyms:OGD1
Ordered Locus Names:YIL125W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1014 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). Ref.1 Ref.4 Ref.5

Catalytic activity

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactor

Thiamine pyrophosphate.

Enzyme regulation

Catabolite repressed.

Subcellular location

Mitochondrion matrix. Mitochondrion matrixmitochondrion nucleoid Ref.5 Ref.6 Ref.8.

Miscellaneous

Present with 14300 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the alpha-ketoglutarate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion Potential
Chain31 – 10149842-oxoglutarate dehydrogenase, mitochondrial
PRO_0000020436

Experimental info

Sequence conflict325 – 3273SEF → LNL in AAA34721. Ref.1
Sequence conflict5131Q → R in AAA34721. Ref.1
Sequence conflict5681A → T in AAA34721. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P20967 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: EF987C4DECE3F09F

FASTA1,014114,416
        10         20         30         40         50         60 
MLRFVSSQTC RYSSRGLLKT SLLKNASTVK IVGRGLATTG TDNFLSTSNA TYIDEMYQAW 

        70         80         90        100        110        120 
QKDPSSVHVS WDAYFKNMSN PKIPATKAFQ APPSISNFPQ GTEAAPLGTA MTGSVDENVS 

       130        140        150        160        170        180 
IHLKVQLLCR AYQVRGHLKA HIDPLGISFG SNKNNPVPPE LTLDYYGFSK HDLDKEINLG 

       190        200        210        220        230        240 
PGILPRFARD GKSKMSLKEI VDHLEKLYCS SYGVQYTHIP SKQKCDWLRE RIEIPEPYQY 

       250        260        270        280        290        300 
TVDQKRQILD RLTWATSFES FLSTKFPNDK RFGLEGLESV VPGIKTLVDR SVELGVEDIV 

       310        320        330        340        350        360 
LGMAHRGRLN VLSNVVRKPN ESIFSEFKGS SARDDIEGSG DVKYHLGMNY QRPTTSGKYV 

       370        380        390        400        410        420 
NLSLVANPSH LESQDPVVLG RTRALLHAKN DLKEKTKALG VLLHGDAAFA GQGVVYETMG 

       430        440        450        460        470        480 
FLTLPEYSTG GTIHVITNNQ IGFTTDPRFA RSTPYPSDLA KAIDAPIFHV NANDVEAVTF 

       490        500        510        520        530        540 
IFNLAAEWRH KFHTDAIIDV VGWRKHGHNE TDQPSFTQPL MYKKIAKQKS VIDVYTEKLI 

       550        560        570        580        590        600 
SEGTFSKKDI DEHKKWVWNL FEDAFEKAKD YVPSQREWLT AAWEGFKSPK ELATEILPHE 

       610        620        630        640        650        660 
PTNVPESTLK ELGKVLSSWP EGFEVHKNLK RILKNRGKSI ETGEGIDWAT GEALAFGTLV 

       670        680        690        700        710        720 
LDGQNVRVSG EDVERGTFSQ RHAVLHDQQS EAIYTPLSTL NNEKADFTIA NSSLSEYGVM 

       730        740        750        760        770        780 
GFEYGYSLTS PDYLVMWEAQ FGDFANTAQV IIDQFIAGGE QKWKQRSGLV LSLPHGYDGQ 

       790        800        810        820        830        840 
GPEHSSGRLE RFLQLANEDP RYFPSEEKLQ RQHQDCNFQV VYPTTPANLF HILRRQQHRQ 

       850        860        870        880        890        900 
FRKPLALFFS KQLLRHPLAR SSLSEFTEGG FQWIIEDIEH GKSIGTKEET KRLVLLSGQV 

       910        920        930        940        950        960 
YTALHKRRES LGDKTTAFLK IEQLHPFPFA QLRDSLNSYP NLEEIVWCQE EPLNMGSWAY 

       970        980        990       1000       1010 
TEPRLHTTLK ETDKYKDFKV RYCGRNPSGA VAAGSKSLHL AEEDAFLKDV FQQS 

« Hide

References

« Hide 'large scale' references
[1]"Structure and regulation of KGD1, the structural gene for yeast alpha-ketoglutarate dehydrogenase."
Repetto B., Tzagoloff A.
Mol. Cell. Biol. 9:2695-2705(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 208353 / W303-1A.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The ogd1 and kgd1 mutants lacking 2-oxoglutarate dehydrogenase activity in yeast are allelic and can be differentiated by the cloned amber suppressor."
Mockovciakova D., Janitorova V., Zigova M., Kaclikova E., Zagulski M., Subik J.
Curr. Genet. 24:377-381(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Identification of the YMN-1 antigen protein and biochemical analyses of protein components in the mitochondrial nucleoid fraction of the yeast Saccharomyces cerevisiae."
Sato H., Tachifuji A., Tamura M., Miyakawa I.
Protoplasma 219:51-58(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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].
[8]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26390 Genomic DNA. Translation: AAA34721.1.
Z46833 Genomic DNA. Translation: CAA86867.1.
BK006942 Genomic DNA. Translation: DAA08428.1.
PIRDEBY. S49884.
RefSeqNP_012141.1. NM_001179473.1.

3D structure databases

ProteinModelPortalP20967.
SMRP20967. Positions 124-1011.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34866. 48 interactions.
DIPDIP-365N.
IntActP20967. 35 interactions.
MINTMINT-623074.
STRING4932.YIL125W.

Proteomic databases

MaxQBP20967.
PaxDbP20967.
PeptideAtlasP20967.
PRIDEP20967.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL125W; YIL125W; YIL125W.
GeneID854681.
KEGGsce:YIL125W.

Organism-specific databases

CYGDYIL125w.
SGDS000001387. KGD1.

Phylogenomic databases

eggNOGCOG0567.
GeneTreeENSGT00530000063092.
HOGENOMHOG000259586.
KOK00164.
OMAQHAPNKE.
OrthoDBEOG72G1GM.

Enzyme and pathway databases

BioCycYEAST:YIL125W-MONOMER.

Gene expression databases

GenevestigatorP20967.

Family and domain databases

Gene3D3.40.50.970. 2 hits.
InterProIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERPTHR23152. PTHR23152. 1 hit.
PfamPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetSearch...

Other

NextBio977289.
PROP20967.

Entry information

Entry nameODO1_YEAST
AccessionPrimary (citable) accession number: P20967
Secondary accession number(s): D6VVG2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

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

Yeast

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

SIMILARITY comments

Index of protein domains and families