2-oxoglutarate dehydrogenase, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P20967 (ODO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [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.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 matrix › mitochondrion 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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion Mitochondrion nucleoid
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Traceable author statement PubMed 9175438. Source: SGD tricarboxylic acid cycle Traceable author statement PubMed 9175438. Source: SGD
Cellular_component	mitochondrial nucleoid Inferred from direct assay Ref.5 PubMed 15692048. Source: SGD mitochondrial oxoglutarate dehydrogenase complex Inferred from direct assay PubMed 2072900. Source: SGD
Molecular_function	oxoglutarate dehydrogenase (succinyl-transferring) activity Traceable author statement PubMed 9175438. Source: SGD thiamine 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

Mitochondrion Potential

Chain

31 – 1014

984

2-oxoglutarate dehydrogenase, mitochondrial

PRO_0000020436

Amino acid modifications

Modified residue

901

Phosphotyrosine Ref.9

Experimental info

Sequence conflict

325 – 327

SEF → LNL in AAA34721. Ref.1

Sequence conflict

513

Q → R in AAA34721. Ref.1

Sequence conflict

568

A → T in AAA34721. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P20967 [UniParc].

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

« Hide

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] [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. Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-901, MASS SPECTROMETRY.
+	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.
PIR	DEBY. S49884.
RefSeq	NP_012141.1. NM_001179473.1.
3D structure databases
ProteinModelPortal	P20967.
SMR	P20967. Positions 124-1011.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-365N.
IntAct	P20967. 44 interactions.
MINT	MINT-623074.
STRING	4932.YIL125W.
Proteomic databases
PaxDb	P20967.
PeptideAtlas	P20967.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIL125W; YIL125W; YIL125W.
GeneID	854681.
KEGG	sce:YIL125W.
Organism-specific databases
CYGD	YIL125w.
SGD	S000001387. KGD1.
Phylogenomic databases
eggNOG	COG0567.
GeneTree	ENSGT00530000063092.
HOGENOM	HOG000259586.
KO	K00164.
OMA	IIKRGGA.
OrthoDB	EOG4GF6P6.
Gene expression databases
ArrayExpress	P20967.
Genevestigator	P20967.
GermOnline	YIL125W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...
Other
NextBio	977289.

Entry information

Entry name

ODO1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome IX

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents