Q8NRC3 (ODO12_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-oxoglutarate dehydrogenase E1/E2 component
Short name=ODH E1/E2 component

Including the following 2 domains:

1. 2-oxoglutarate dehydrogenase E1 component
   Short name=ODH E1 component
   EC=1.2.4.2
   Alternative name(s):
   Alpha-ketoglutarate dehydrogenase E1 component
   Short name=KDH E1 component
2. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
   EC=2.3.1.61
   Alternative name(s):
   2-oxoglutarate dehydrogenase complex E2 component
   Short name=ODH E2 component
   Short name=OGDC-E2
   Dihydrolipoamide succinyltransferase

Gene names

Name:	odhA
Ordered Locus Names:	Cgl1129, cg1280

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › Corynebacterium glutamicum

Protein attributes

Sequence length	1221 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	Catalyzes the E1 and E2 reactions as part of 2-oxoglutarate dehydrogenase (ODH) activity, to convert 2-oxoglutarate to succinyl-CoA and CO2. OdhA has reductase activity with 2-oxoglutarate but does not react with pyruvate, and also displays transsuccinylase but no transacetylase activity. Since OdhA is not lipoylated, the succinyltransferase activity of its E2 domain is dependent on lipoyl residues of the acetyltransferase AceF. Ref.4
Catalytic activity	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. Ref.1 Ref.4 Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. Ref.1 Ref.4
Cofactor	Magnesium By similarity. Thiamine pyrophosphate By similarity. UniProtKB P0AFG3
Enzyme regulation	Inhibited by unphosphorylated OdhI, but not by phosphorylated OdhI. Ref.5 Ref.7
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
Subunit structure	Homodimer By similarity. Makes part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2). Interacts with the FHA domain of unphosphorylated OdhI via its C-terminal dehydrogenase domain. Ref.5 Ref.7 UniProtKB P0AFG3
Domain	OdhA is a fusion protein with two major domains exhibiting structural features of an E1 and E2 protein, and a short sequence stretch of E1 localized at the N-terminus, which is connected by a linker region to the rest of the protein. Deletion of individual parts of odhA show that all parts of odhA are required for a functional tricarboxylic acid cycle in C.glutamicum; the ODH activity is in fact completely abolished in each of these mutants, and the PDH activity is significantly reduced, which could indicate that the overall structure of the supercomplex is disturbed. Ref.4 Ref.7
Disruption phenotype	Strains lacking this gene completely lack 2-oxoglutarate dehydrogenase activity. Deletion of odhA also causes L-glutamate overproduction and accumulation during growth. Ref.6
Miscellaneous	Is non-lipoylated. In contrast, the E2 component AceF is the prominent lipoylated protein in C.glutamicum.
Sequence similarities	In the N-terminal section; belongs to the alpha-ketoglutarate dehydrogenase family. In the C-terminal section; belongs to the 2-oxoacid dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=0.014 mM for 2-oxoglutarate Ref.4
Sequence caution	The sequence BAB98522.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAF19835.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Acyltransferase Oxidoreductase Transferase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine 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
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 1221	1220	2-oxoglutarate dehydrogenase E1/E2 component		PRO_0000273521
Regions
	Region	2 – 40	39	2-oxoglutarate dehydrogenase E1, N-terminal part
	Region	41 – 89	49	Linker
	Region	90 – 337	248	Succinyltransferase E2
	Region	338 – 1221	884	2-oxoglutarate dehydrogenase E1, C-terminal part
	Region	543 – 544	2	Thiamine pyrophosphate binding By similarity
	Region	608 – 610	3	Thiamine pyrophosphate binding By similarity
	Region	645 – 647	3	Thiamine pyrophosphate binding By similarity
Sites
	Active site	316	1	Proton acceptor; for succinyltransferase activity Ref.4
	Metal binding	645	1	Magnesium By similarity
	Metal binding	678	1	Magnesium By similarity
	Metal binding	680	1	Magnesium; via carbonyl oxygen By similarity
	Binding site	583	1	2-oxoglutarate By similarity
	Binding site	608	1	2-oxoglutarate By similarity
	Binding site	949	1	Thiamine pyrophosphate By similarity
	Binding site	1017	1	2-oxoglutarate By similarity
Experimental info
	Mutagenesis	258	1	T → A: Loss of E2 succinyltransferase activity, but nearly no effect on E1 dehydrogenase activity. Ref.4
	Mutagenesis	316	1	H → C: Loss of E2 succinyltransferase activity, and 2-fold reduction in E1 dehydrogenase activity. Ref.4
	Mutagenesis	320	1	Q → D: Slight reduction in E2 succinyltransferase activity and in E1 dehydrogenase activity. Ref.4
	Sequence conflict	44	1	T → A in BAA12222. Ref.1
	Sequence conflict	82	1	D → A in BAA12222. Ref.1
	Sequence conflict	238	1	A → T in BAA12222. Ref.1
	Sequence conflict	413	1	N → S in BAA12222. Ref.1
	Sequence conflict	424	1	N → S in BAA12222. Ref.1
	Sequence conflict	967	1	I → V in BAA12222. Ref.1
	Sequence conflict	1093	1	N → D in BAA12222. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8NRC3 [UniParc]. Last modified November 28, 2012. Version 2. Checksum: BF0A1827EA1B0080	FASTA	1,221	134,664
	10 20 30 40 50 60 MSSASTFGQN AWLVDEMFQQ FQKDPKSVDK EWRELFEAQG GPNTTPATTE AQPSAPKESA 70 80 90 100 110 120 KPAPKAAPAA KAAPRVETKP ADKTAPKAKE SSVPQQPKLP EPGQTPIRGI FKSIAKNMDI 130 140 150 160 170 180 SLEIPTATSV RDMPARLMFE NRAMVNDQLK RTRGGKISFT HIIGYAMVKA VMAHPDMNNS 190 200 210 220 230 240 YDVIDGKPTL IVPEHINLGL AIDLPQKDGS RALVVAAIKE TEKMNFSEFL AAYEDIVARS 250 260 270 280 290 300 RKGKLTMDDY QGVTVSLTNP GGIGTRHSVP RLTKGQGTII GVGSMDYPAE FQGASEDRLA 310 320 330 340 350 360 ELGVGKLVTI TSTYDHRVIQ GAVSGEFLRT MSRLLTDDSF WDEIFDAMNV PYTPMRWAQD 370 380 390 400 410 420 VPNTGVDKNT RVMQLIEAYR SRGHLIADTN PLSWVQPGMP VPDHRDLDIE THNLTIWDLD 430 440 450 460 470 480 RTFNVGGFGG KETMTLREVL SRLRAAYTLK VGSEYTHILD RDERTWLQDR LEAGMPKPTQ 490 500 510 520 530 540 AEQKYILQKL NAAEAFENFL QTKYVGQKRF SLEGAEALIP LMDSAIDTAA GQGLDEVVIG 550 560 570 580 590 600 MPHRGRLNVL FNIVGKPLAS IFNEFEGQME QGQIGGSGDV KYHLGSEGQH LQMFGDGEIK 610 620 630 640 650 660 VSLTANPSHL EAVNPVMEGI VRAKQDYLDK GVDGKTVVPL LLHGDAAFAG LGIVPETINL 670 680 690 700 710 720 AKLRGYDVGG TIHIVVNNQI GFTTTPDSSR SMHYATDYAK AFGCPVFHVN GDDPEAVVWV 730 740 750 760 770 780 GQLATEYRRR FGKDVFIDLV CYRLRGHNEA DDPSMTQPKM YELITGRETV RAQYTEDLLG 790 800 810 820 830 840 RGDLSNEDAE AVVRDFHDQM ESVFNEVKEG GKKQAEAQTG ITGSQKLPHG LETNISREEL 850 860 870 880 890 900 LELGQAFANT PEGFNYHPRV APVAKKRVSS VTEGGIDWAW GELLAFGSLA NSGRLVRLAG 910 920 930 940 950 960 EDSRRGTFTQ RHAVAIDPAT AEEFNPLHEL AQSKGNNGKF LVYNSALTEY AGMGFEYGYS 970 980 990 1000 1010 1020 VGNEDSIVAW EAQFGDFANG AQTIIDEYVS SGEAKWGQTS KLILLLPHGY EGQGPDHSSA 1030 1040 1050 1060 1070 1080 RIERFLQLCA EGSMTVAQPS TPANHFHLLR RHALSDLKRP LVIFTPKSML RNKAAASAPE 1090 1100 1110 1120 1130 1140 DFTEVTKFQS VINDPNVADA AKVKKVMLVS GKLYYELAKR KEKDGRDDIA IVRIEMLHPI 1150 1160 1170 1180 1190 1200 PFNRISEALA GYPNAEEVLF VQDEPANQGP WPFYQEHLPE LIPNMPKMRR VSRRAQSSTA 1210 1220 TGVAKVHQLE EKQLIDEAFE A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the Corynebacterium glutamicum ('Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase." Usuda Y., Tujimoto N., Abe C., Asakura Y., Kimura E., Kawahara Y., Kurahashi O., Matsui H. Microbiology 142:3347-3354(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY. Strain: AJ12036.
[2]	"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceF." Hoffelder M., Raasch K., van Ooyen J., Eggeling L. J. Bacteriol. 192:5203-5211(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, FUNCTION AS E1 AND E2 COMPONENT OF ODH, CATALYTIC ACTIVITY, KINETIC PARAMETERS, DOMAIN, LACK OF LIPOYLATION, ACTIVE SITE, MUTAGENESIS OF THR-258; HIS-316 AND GLN-320. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[5]	"Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein." Niebisch A., Kabus A., Schultz C., Weil B., Bott M. J. Biol. Chem. 281:12300-12307(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INHIBITION BY ODHI, IDENTIFICATION IN THE ODH/PDH COMPLEX. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[6]	"Altered metabolic flux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum." Asakura Y., Kimura E., Usuda Y., Kawahara Y., Matsui K., Osumi T., Nakamatsu T. Appl. Environ. Microbiol. 73:1308-1319(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE. Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[7]	"The FHA domain of OdhI interacts with the carboxyterminal 2-oxoglutarate dehydrogenase domain of OdhA in Corynebacterium glutamicum." Krawczyk S., Raasch K., Schultz C., Hoffelder M., Eggeling L., Bott M. FEBS Lett. 584:1463-1468(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, ENZYME REGULATION, INTERACTION WITH ODHI. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D84102 Genomic DNA. Translation: BAA12222.2. BA000036 Genomic DNA. Translation: BAB98522.1. Different initiation. BX927151 Genomic DNA. Translation: CAF19835.1. Different initiation.
RefSeq	NP_600357.3. NC_003450.3. YP_225421.2. NC_006958.1.
3D structure databases
ProteinModelPortal	Q8NRC3.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg1280.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB98522; BAB98522; BAB98522. CAF19835; CAF19835; cg1280.
GeneID	1019114. 3343144.
KEGG	cgb:cg1280. cgl:NCgl1084.
PATRIC	21494302. VBICorGlu203724_1108.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000259587.
KO	K00164.
ProtClustDB	PRK12270.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-1116-MONOMER.
UniPathway	UPA00223; UER00997.
Family and domain databases
Gene3D	3.30.559.10. 1 hit.
InterPro	IPR001078. 2-oxoacid_DH_actylTfrase. IPR011603. 2oxoglutarate_DH_E1. IPR023213. CAT-like_dom. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. 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

ODO12_CORGL

Accession

Primary (citable) accession number: Q8NRC3
Secondary accession number(s): P96746, Q6M641

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	November 28, 2012
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program