Reviewed, UniProtKB/Swiss-Prot Q02218 (ODO1_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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.

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). 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 + CO(2).
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.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Ubl conjugation
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 40	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)
Experimental info
	Sequence conflict	730 – 733	4	LGFA → AGLR in BAA01393. Ref.1
	Sequence conflict	730 – 733	4	LGFA → AGLR in BAA06836. Ref.2
	Sequence conflict	831	1	N → D in BAA06836. Ref.2
	Sequence conflict	989	1	D → N in BAA01393. Ref.1
	Sequence conflict	989	1	D → N in BAA06836. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q02218-1 [UniParc]. Last modified November 13, 2007. Version 3. Checksum: F428DD342F232E7C	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

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. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., 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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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.
+	Additional computationally mapped references.

Web resources

Wikipedia

Alpha-ketoglutarate dehydrogenase entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	A38234.
RefSeq	NP_001003941.1. NP_002532.2.
UniGene	Hs.488181
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02218.
PTM databases
PhosphoSite	Q02218.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00098902.
Genome annotation databases
Ensembl	ENSG00000105953. Homo sapiens. [Contig view]
GeneID	4967.
KEGG	hsa:4967.
Organism-specific databases
H-InvDB	HIX0006651.
HGNC	HGNC:8124. OGDH.
HPA	HPA019514.
MIM	203740. gene+phenotype.
Orphanet	31. Oxoglutaricaciduria.
PharmGKB	PA31910.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	Q02218.
Enzyme and pathway databases
Reactome	REACT_1046. Pyruvate metabolism and TCA cycle. REACT_13. Metabolism of amino acids.
Gene expression databases
ArrayExpress	Q02218.
CleanEx	HS_OGDH.
GermOnline	ENSG00000105953. Homo sapiens.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DHase_E1. IPR001017. DHase_E1. IPR005475. Transketo_Cen_R. [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.
SOURCE	Search...

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:	November 25, 2008
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)