Reviewed, UniProtKB/Swiss-Prot Q623T0 (ODO1_CAEBR)

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

ORF Names:

CBG01737

Organism

Caenorhabditis briggsae [Complete proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	1027 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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. UniProtKB Q02218
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. UniProtKB Q02218
Cofactor	Thiamine pyrophosphate By similarity. UniProtKB Q02218
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
Technical term	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 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 – ?		Mitochondrion
	Chain	? – 1027		2-oxoglutarate dehydrogenase E1 component, mitochondrial		PRO_0000234099

Sequences

	Sequence		Length	Mass (Da)
	Q623T0-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 99584397C5540D7B	FASTA	1,027	115,481
	10 20 30 40 50 60 MHRASLICRL ASPSRINSIR SASSYGNNTI SATPLVQQRK QSVAASVKHE PFLNGSSSVY 70 80 90 100 110 120 IEQMYETWLE NPSSVHTSWD AYFRNVEAGA GPGQAFQAPP SVAYAGSMGV PSAPITSAAP 130 140 150 160 170 180 ATRLDTNASV QSISDHLKIQ LLIRSYQTRG HNIADLDPLG INSADLDDTI PPELELSFYG 190 200 210 220 230 240 LGERDLDREF LLPPTTFISE KKSLTLREIL QRLKEIYCTS TGVEYMHLNN LEQQDWIRRR 250 260 270 280 290 300 FEAPRVTELS HDQKKVLFKR LIRSTKFEEF LAKKWPSEKR FGLEGCEVLI PAIKQVIDSS 310 320 330 340 350 360 STLGVDSFVI GMPHRGRLNV LANVCRQPLA TILSQFSTLE PADEGSGDVK YHLGVCIERL 370 380 390 400 410 420 NRQSQKNVKI AVVANPSHLE AVDPVVMGKV RAEAFYAGDE KCDRTMAILL HGDAAFAGQG 430 440 450 460 470 480 VVLETFNLDD LPSYTTHGAI HIVVNNQIGF TTDPRSSRSS PYCTDVGRVV GCPIFHVNVD 490 500 510 520 530 540 DPEAVMHVCN VAADWRKTFK KDVIVDLVCY RRHGHNELDE PMFTQPLMYQ RIKQTKTALE 550 560 570 580 590 600 KYQEKILNEG VANEQYVKEE LTKYGAILED AYENAQKVTY VRNRDWLDSP WDDFFKKRDP 610 620 630 640 650 660 LKLPSTGIEQ ENIEHIIGKF GSYPEGFNLH RGLERTLKGR QQMLKDNSLD WACGEALAFG 670 680 690 700 710 720 SLLKEGIHVR LSGQDVERGT FSHRHHVLHD QKVDQKIYNP LNDLADPQGE YTVCNSSLSE 730 740 750 760 770 780 YAVLGFELGY SMVDPNSLVI WEAQFGDFSN TAQCIIDQFV SSGQSKWIRQ SGLVMLLPHG 790 800 810 820 830 840 YEGMGPEHSS ARPERFLQMC NEDDEIDLDK IAFGGTFEAQ QLHDTNWIVA NCTTPANIYH 850 860 870 880 890 900 LLRRQVTMPF RKPAVVFSPK SLLRHPMARS PVEDFQSGSN FQRIIPETGA PSQNPPNVQR 910 920 930 940 950 960 LVFCTGKVYY DMVAARKHVG KENDVALVRV EQLSPFPYDL VQQECRKYQG AEIIWAQEEH 970 980 990 1000 1010 1020 KNMGAWSFVQ PRINSLLSID GRATKYAGRL PSSSPATGNK YTHMQEQKEM MSKVFGVPKS KLEGFKA

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CAAC02000447 Genomic DNA. Translation: CAP22897.1.
3D structure databases
ModBase	Search...
Organism-specific databases
WormBase	WBGene00024926. CBG01737.
Phylogenomic databases
OMA	Q623T0. PRIRTTI.
Enzyme and pathway databases
BRENDA	1.2.4.2. 261794.
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...

Entry information

Entry name

ODO1_CAEBR

Accession

Primary (citable) accession number: Q623T0
Secondary accession number(s): A8WQY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	November 23, 2004
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project