2-oxoglutarate dehydrogenase E1 component, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot Q02218 (ODO1_HUMAN)

Last modified July 7, 2009. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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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:

OGDH

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	1023 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO₂.
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	Catabolite repressed.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.
Sequence caution	The sequence BAA01393.1 differs from that shown. Reason: Frameshift at position 1003. The sequence BAA06836.1 differs from that shown. Reason: Frameshift at position 1003.

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Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from Experiment. Source: Reactome mitochondrial membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from sequence or structural similarity. Source: UniProtKB thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 40

Mitochondrion

Chain

41 – 1023

983

2-oxoglutarate dehydrogenase E1 component, mitochondrial

PRO_0000020432

Amino acid modifications

Cross-link

534

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Natural variations

Natural variant

1018

V → I: dbSNP rs2070607.

VAR_050435

Experimental info

Sequence conflict

730 – 733

LGFA → AGLR in BAA01393. Ref.1

Sequence conflict

730 – 733

LGFA → AGLR in BAA06836. Ref.2

Sequence conflict

831

N → D in BAA06836. Ref.2

Sequence conflict

989

D → N in BAA01393. Ref.1

Sequence conflict

989

D → N in BAA06836. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q02218-1 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: F428DD342F232E7C
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FASTA

1,023

115,935

        10         20         30         40         50         60 
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE 

        70         80         90        100        110        120 
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV 

       130        140        150        160        170        180 
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES 

       190        200        210        220        230        240 
DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 

       250        260        270        280        290        300 
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN 

       310        320        330        340        350        360 
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR 

       370        380        390        400        410        420 
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV 

       430        440        450        460        470        480 
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP 

       490        500        510        520        530        540 
EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 

       550        560        570        580        590        600 
AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR 

       610        620        630        640        650        660 
SMSCPSTGLT EDILTHIGNV ASSVPVENFT IHGGLSRILK TRGEMVKNRT VDWALAEYMA 

       670        680        690        700        710        720 
FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 

       730        740        750        760        770        780 
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP 

       790        800        810        820        830        840 
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH 

       850        860        870        880        890        900 
VLRRQILLPF RKPLIIFTPK SLLRHPEARS SFDEMLPGTH FQRVIPEDGP AAQNPENVKR 

       910        920        930        940        950        960 
LLFCTGKVYY DLTRERKARD MVGQVAITRI EQLSPFPFDL LLKEVQKYPN AELAWCQEEH 

       970        980        990       1000       1010       1020 
KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDVFK 


NFS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequence of the cDNA encoding human 2-oxoglutarate dehydrogenase (lipoamide)." Koike K., Urata Y., Goto S. Proc. Natl. Acad. Sci. U.S.A. 89:1963-1967(1992) [PubMed: 1542694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The gene encoding human 2-oxoglutarate dehydrogenase: structural organization and mapping to chromosome 7p13-p14." Koike K. Gene 159:261-266(1995) [PubMed: 7622061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[6]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-534, MASS SPECTROMETRY.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

Wikipedia

Alpha-ketoglutarate dehydrogenase entry

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Cross-references

Sequence databases

D10523 mRNA. Translation: BAA01393.1. Frameshift.
D32064 Genomic DNA. Translation: BAA06836.1. Frameshift.
AC004859 Genomic DNA. Translation: AAQ96885.1.
CH471128 Genomic DNA. Translation: EAW61086.1.
BC004964 mRNA. Translation: AAH04964.1.
BC014617 mRNA. Translation: AAH14617.1.

IPI

IPI00098902.

PIR

A38234.

RefSeq

NP_001003941.1.
NP_002532.2.

UniGene

Hs.488181

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ERY	X-ray	1.95	P/Q	932-940	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02218. 2 interactions.

PTM databases

PhosphoSite

Q02218.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00098902.

Proteomic databases

PRIDE

Q02218.

Genome annotation databases

Ensembl

ENSG00000105953. Homo sapiens. [Contig view]

GeneID

4967.

KEGG

hsa:4967.

UCSC

uc003tln.1. human.

Organism-specific databases

GeneCards

GC07P044612.

H-InvDB

HIX0006651.

HGNC

HGNC:8124. OGDH.

HPA

HPA019514.

MIM

203740. gene+phenotype.

Orphanet

31. Oxoglutaricaciduria.

PharmGKB

PA31910.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q02218.

OMA

Q02218. PRIRTTI.

Enzyme and pathway databases

BRENDA

1.2.4.2. 247.

Reactome

REACT_1046. Pyruvate metabolism and TCA cycle.
REACT_13. Metabolism of amino acids.
REACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.

Gene expression databases

ArrayExpress

Q02218.

Bgee

Q02218.

CleanEx

HS_OGDH.

GermOnline

ENSG00000105953. Homo sapiens.

Family and domain databases

InterPro

IPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR005475. Transketolase_central-reg.
[Graphical view]

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

DrugBank

DB00157. NADH.

NextBio

19110.

PMAP-CutDB

Q02218.

SOURCE

Search...

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Entry information

Entry name

ODO1_HUMAN

Accession

Primary (citable) accession number: Q02218
Secondary accession number(s): Q9UDX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 13, 2007
Last modified:	July 7, 2009
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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