Reviewed, UniProtKB/Swiss-Prot P20707 (ODO1_AZOVI)

Names and origin

Protein names

Recommended name:
    2-oxoglutarate dehydrogenase E1 component
    EC=1.2.4.2
Alternative name(s):
    Alpha-ketoglutarate dehydrogenase

Gene names

Name:	sucA
Synonyms:	odhA

Organism

Azotobacter vinelandii

Taxonomic identifier

354 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter

Protein attributes

Sequence length	943 AA.
Sequence status	Complete.
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).
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC 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
	Chain	1 – 943	943	2-oxoglutarate dehydrogenase E1 component		PRO_0000162186

Sequences

	Sequence		Length	Mass (Da)
	P20707-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: D3F35356D454E2A1	FASTA	943	105,688
	10 20 30 40 50 60 MQDSVMQRMW NSAHLSGGNA AYVEELYELY LHDPNAVPEE WRTYFEKLPA EAGTSTDVPH 70 80 90 100 110 120 APVRDQFVLL AKNQRRAQPV ATSSVSTEHE KKQVEVLRLI QAYRTRGHQA SQLDPLGLWQ 130 140 150 160 170 180 RTAPSDLSIT HYGLTNADLD TPFRTGELYI GKEEATLREI LQALQETYCR TIGAEFTHIV 190 200 210 220 230 240 DSEQRNWFAQ RLESVRGRPV YSKEAKSHLL ERLSAAEGLE KYLGTKYPGT KRFGLEGGES 250 260 270 280 290 300 LVPVVDEIIQ RSGSYGTKEV VIGMAHRGRL NLLVNALGKN PRDLFDEFEG KHLVELGSGD 310 320 330 340 350 360 VKYHQGFSSN VMTSGGEVHL AMAFNPSHLE IVSPVVEGSV RARQDRRVDA TGEKVVPISI 370 380 390 400 410 420 HGDSAFAGQG VVMETFQMSQ IRGYKTGGTI HIVVNNQVGF TTSNPVDTRS TEYCTDPAKM 430 440 450 460 470 480 IQAPVLHVNG DDPEAVLFVT QLAVDYRMQF KRDVVIDLVC YRRRGHNEAD EPSGTQPLMY 490 500 510 520 530 540 QKIAKQPTTR ELYADALVKE GSLSQEEVQA KVDEYRTALD NGQHVLKSLV KEPNTELFVD 550 560 570 580 590 600 WTPYLGHAWT ARHDTSFELK TLQELNAKLL QIPEGFVVQR QVAKILEDRG RMGVGAMPIN 610 620 630 640 650 660 WGCAETLAYA TLLKEGHPVR ITGQDVGRGT FSHRHAALHN QKDASRYIPL QNLYEGQPKF 670 680 690 700 710 720 ELYDSFLSEE AVLAFEYGYA TTTPNALVIW EASSGDFANG AQVVIDQFIS SGETKWGALC 730 740 750 760 770 780 GLTMLLPHGY EGQGPEHSSA RLERYLQLCA EQNIQVCVPT TPAQVYHMLR RQVIRPLRKP 790 800 810 820 830 840 LVALTPKSLL RHKSAISTLE DLALGSFHPV LPEVDSLDPK KVERLVLCSG KVYYDLLDKR 850 860 870 880 890 900 HAEGREDIAI VRIEQLYPFP EEELAEVMAP YTNLKHVVWC QEEPMNQGAW YCSQHHMRRV 910 920 930 940 ASAHKKELFL QYAGREASAA PACGYASMHA EQQEKLLQDA FTV

References

[1]	"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component." Schulze E., Westphal A.H., Hanemaaijer R., de Kok A. Eur. J. Biochem. 187:229-234(1990) [PubMed: 2404759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component." Westphal A.H., de Kok A. Eur. J. Biochem. 187:235-239(1990) [PubMed: 2404760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 909-943.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52433 Genomic DNA. Translation: CAA36680.1. X52432 Genomic DNA. Translation: CAA36677.1.
PIR	S07776.
3D structure databases
SMR	P20707. Positions 90-943.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.4.2. 883.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [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.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODO1_AZOVI

Accession

Primary (citable) accession number: P20707

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	February 9, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)