Reviewed, UniProtKB/Swiss-Prot Q5XI78 (ODO1_RAT)

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
Synonyms:	Ogdhl

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Enzyme regulation	Catabolite repressed By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from direct assay. Source: RGD NADH metabolic process Inferred from direct assay. Source: RGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW succinyl-CoA metabolic process Inferred from direct assay. Source: RGD tricarboxylic acid cycle Inferred from direct assay. Source: RGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial membrane Inferred from sequence or structural similarity. Source: UniProtKB oxoglutarate dehydrogenase complex Inferred from direct assay. Source: RGD
Molecular function	chaperone binding Inferred from physical interaction. Source: RGD heat shock protein binding Inferred from physical interaction. Source: RGD 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 By similarity
	Chain	41 – 1023	983	2-oxoglutarate dehydrogenase E1 component, mitochondrial		PRO_0000271367
Amino acid modifications
	Cross-link	534		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5XI78-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: B258886383FBD98C	FASTA	1,023	116,296
	10 20 30 40 50 60 MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE 70 80 90 100 110 120 MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV 130 140 150 160 170 180 DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES 190 200 210 220 230 240 DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 250 260 270 280 290 300 PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN 310 320 330 340 350 360 GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH 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 AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 550 560 570 580 590 600 AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR 610 620 630 640 650 660 SMTCPSTGLE EDILTHIGNV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA 670 680 690 700 710 720 FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 730 740 750 760 770 780 SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP 790 800 810 820 830 840 HGMEGMGPEH SSARPERFLQ MCNDDPDVLP NLQEENFDIS QLYDCNWIVV NCSTPGNFFH 850 860 870 880 890 900 VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPEDGP AAQNPDKVKR 910 920 930 940 950 960 LLFCTGKVYY DLTRERKARD MAEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH 970 980 990 1000 1010 1020 KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK KFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Kidney.
[2]	Lubec G., Afjehi-Sadat L. Submitted (DEC-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 82-101; 123-135; 172-184 AND 583-600, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC083811 mRNA. Translation: AAH83811.1.
IPI	IPI00215093.
RefSeq	NP_001017461.1.
UniGene	Rn.45991
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q5XI78.
Genome annotation databases
Ensembl	ENSRNOG00000005130. Rattus norvegicus. [Contig view]
GeneID	360975.
KEGG	rno:360975.
NMPDR	fig|10116.3.peg.10710.
Organism-specific databases
RGD	1561359. Ogdh.
Phylogenomic databases
HOVERGEN	Q5XI78.
Enzyme and pathway databases
BRENDA	1.2.4.2. 248.
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	674779.

Entry information

Entry name

ODO1_RAT

Accession

Primary (citable) accession number: Q5XI78

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	November 23, 2004
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)