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Q8NNJ2 (ODP2_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

EC=2.3.1.12
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2
Short name=PDH component E2
Gene names
Name:aceF
Synonyms:sucB
Ordered Locus Names:Cgl2207, cg2421
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is essential for both 2-oxoglutarate dehydrogenase (ODH) and pyruvate dehydrogenase (PDH) activities, but AceF has exclusively transacetylase (and no transsuccinylase) activity. The lipoyl residues required for ODH activity are likely provided by AceF. Ref.4

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. Ref.4

Cofactor

Binds 3 lipoyl cofactors covalently Probable. Ref.4

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. Part of an unusual ODH/PDH supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together with OdhA (E1+E2). Ref.3

Disruption phenotype

Cells lacking this gene display no ODH and no PDH activities. Ref.4

Miscellaneous

Is the only lipoylated protein in C.glutamicum.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 E3-binding domain.

Contains 3 lipoyl-binding domains.

Ontologies

Keywords
   Biological processGlycolysis
Tricarboxylic acid cycle
   DomainLipoyl
Repeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiondihydrolipoyllysine-residue acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 675675Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
PRO_0000420521

Regions

Domain3 – 7674Lipoyl-binding 1
Domain122 – 19574Lipoyl-binding 2
Domain238 – 31174Lipoyl-binding 3
Domain371 – 40737E3-binding
Compositional bias81 – 351271Glu-rich

Sites

Active site6451 By similarity
Active site6491 By similarity

Amino acid modifications

Modified residue431N6-lipoyllysine Probable
Modified residue1621N6-lipoyllysine Probable
Modified residue2781N6-lipoyllysine Probable

Experimental info

Mutagenesis431K → Q: No effect on ODH and PDH activity; when associated with Q-162. Ref.4
Mutagenesis1621K → Q: No effect on ODH and PDH activity; when associated with Q-43. Strong reduction in the catalytic efficiency of ODH and slight reduction in that of PDH; when associated with Q-278. Ref.4
Mutagenesis2781K → Q: Strong reduction in the catalytic efficiency of ODH and slight reduction in that of PDH; when associated with Q-162. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8NNJ2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 1D262FA89899B47F

FASTA67570,905
        10         20         30         40         50         60 
MAFSVEMPEL GESVTEGTIT QWLKSVGDTV EVDEPLLEVS TDKVDTEIPS PVAGVILEIK 

        70         80         90        100        110        120 
AEEDDTVDVG GVIAIIGDAD ETPANEAPAD EAPAPAEEEE PVKEEPKKEA APEAPAATGA 

       130        140        150        160        170        180 
ATDVEMPELG ESVTEGTITQ WLKAVGDTVE VDEPLLEVST DKVDTEIPSP VAGTIVEILA 

       190        200        210        220        230        240 
DEDDTVDVGA VIARIGDANA AAAPAEEEAA PAEEEEPVKE EPKKEAAPEA PAATGAATDV 

       250        260        270        280        290        300 
EMPELGESVT EGTITQWLKA VGDTVEVDEP LLEVSTDKVD TEIPSPVAGT IVEILADEDD 

       310        320        330        340        350        360 
TVDVGAVIAR IGDANAAAAP AEEEAAPAEE EEPVKEEPKK EEPKKEEPKK EAATTPAAAS 

       370        380        390        400        410        420 
ATVSASGDNV PYVTPLVRKL AEKHGVDLNT VTGTGIGGRI RKQDVLAAAN GEAAPAEAAA 

       430        440        450        460        470        480 
PVSAWSTKSV DPEKAKLRGT TQKVNRIREI TAMKTVEALQ ISAQLTQLHE VDMTRVAELR 

       490        500        510        520        530        540 
KKNKPAFIEK HGVNLTYLPF FVKAVVEALV SHPNVNASFN AKTKEMTYHS SVNLSIAVDT 

       550        560        570        580        590        600 
PAGLLTPVIH DAQDLSIPEI AKAIVDLADR SRNNKLKPND LSGGTFTITN IGSEGALSDT 

       610        620        630        640        650        660 
PILVPPQAGI LGTGAIVKRP VVITEDGIDS IAIRQMVFLP LTYDHQVVDG ADAGRFLTTI 

       670 
KDRLETANFE GDLQL 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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. expand/collapse author list , 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.
[3]"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: IDENTIFICATION IN THE ODH/PDH COMPLEX.
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: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, COFACTOR, LIPOYLATION, MUTAGENESIS OF LYS-43; LYS-162 AND LYS-278.
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99600.1.
BX927154 Genomic DNA. Translation: CAF20547.1.
RefSeqNP_601410.1. NC_003450.3.
YP_226448.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NNJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99600; BAB99600; BAB99600.
CAF20547; CAF20547; cg2421.
GeneID1020158.
3344465.
KEGGcgb:cg2421.
cgl:NCgl2126.
PATRIC21496412. VBICorGlu203724_2142.

Phylogenomic databases

HOGENOMHOG000281564.
KOK00658.
OMAFTPIFME.
OrthoDBEOG610413.
ProtClustDBPRK11854.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR014276. 2-oxoglutarate_DH_E2.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsTIGR02927. SucB_Actino. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP2_CORGL
AccessionPrimary (citable) accession number: Q8NNJ2
Secondary accession number(s): Q6M3N0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 1, 2002
Last modified: December 11, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families