Reviewed, UniProtKB/Swiss-Prot P20967 (ODO1_YEAST)

Names and origin

Protein names

Recommended name:
    2-oxoglutarate dehydrogenase E1 component, mitochondrial
    EC=1.2.4.2
Alternative name(s):
    Alpha-ketoglutarate dehydrogenase

Gene names

Name:	KGD1
Synonyms:	OGD1
Ordered Locus Names:	YIL125W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1014 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.3 Ref.4
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 matrix › mitochondrion nucleoid. Ref.4 Ref.5 Ref.7
Miscellaneous	Present with 14300 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Traceable author statement. Source: SGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Traceable author statement. Source: SGD
Cellular component	mitochondrial nucleoid Ref.4 Inferred from direct assay. Source: SGD mitochondrial oxoglutarate dehydrogenase complex Inferred from direct assay. Source: SGD
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Traceable author statement. Source: SGD thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion Potential
	Chain	31 – 1014	984	2-oxoglutarate dehydrogenase E1 component, mitochondrial		PRO_0000020436
Amino acid modifications
	Modified residue	901	1	Phosphotyrosine Ref.8
Experimental info
	Sequence conflict	325 – 327	3	SEF → LNL in AAA34721. Ref.1
	Sequence conflict	513	1	Q → R in AAA34721. Ref.1
	Sequence conflict	568	1	A → T in AAA34721. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P20967-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: EF987C4DECE3F09F	FASTA	1,014	114,416
	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

References

	« Hide 'large scale' referencesShow '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: 2503710] [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. , 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: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 8299151] [Abstract] Cited for: FUNCTION.
[4]	"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: 11926067] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-901, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M26390 Genomic DNA. Translation: AAA34721.1. Z46833 Genomic DNA. Translation: CAA86867.1.
PIR	DEBY. S49884.
RefSeq	NP_012141.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:365N.
IntAct	P20967. 45 interactions.
Proteomic databases
PeptideAtlas	P20967.
PRIDE	P20967.
Genome annotation databases
Ensembl	YIL125W. Saccharomyces cerevisiae. [Contig view]
GeneID	854681.
GenomeReviews	Gene locus YIL125W in contig Z47047_GR.
KEGG	sce:YIL125W.
NMPDR	fig|4932.3.peg.1665.
Organism-specific databases
CYGD	YIL125w.
SGD	S000001387. KGD1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P20967.
OMA	P20967. PRIRTTI.
Enzyme and pathway databases
BRENDA	1.2.4.2. 250.
Gene expression databases
ArrayExpress	P20967.
GermOnline	YIL125W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase_central-reg. [Graphical view]
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	977289.

Entry information

Entry name

ODO1_YEAST

Accession

Primary (citable) accession number: P20967

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)