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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.1 Publication

Cofactori

(R)-lipoate1 PublicationNote: Binds 3 lipoyl cofactors covalently.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei645By similarity1
Active sitei649By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis, Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciCGLU1204414:G134W-2125-MONOMER.
CORYNE:G18NG-11799-MONOMER.
BRENDAi2.3.1.61. 960.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:aceF
Synonyms:sucB
Ordered Locus Names:Cgl2207, cg2421
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene display no ODH and no PDH activities.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43K → Q: No effect on ODH and PDH activity; when associated with Q-162. 1 Publication1
Mutagenesisi162K → 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. 1 Publication1
Mutagenesisi278K → Q: Strong reduction in the catalytic efficiency of ODH and slight reduction in that of PDH; when associated with Q-162. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004205211 – 675Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST675

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-lipoyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei162N6-lipoyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei278N6-lipoyllysinePROSITE-ProRule annotation1 Publication1

Interactioni

Subunit structurei

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).By similarity1 Publication

Protein-protein interaction databases

STRINGi196627.cg2421.

Structurei

3D structure databases

ProteinModelPortaliQ8NNJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 77Lipoyl-binding 1PROSITE-ProRule annotationAdd BLAST76
Domaini121 – 196Lipoyl-binding 2PROSITE-ProRule annotationAdd BLAST76
Domaini237 – 312Lipoyl-binding 3PROSITE-ProRule annotationAdd BLAST76
Domaini371 – 407E3-bindingAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi81 – 351Glu-richAdd BLAST271

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 E3-binding domain.Curated
Contains 3 lipoyl-binding domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Repeat

Phylogenomic databases

eggNOGiCOG0508. LUCA.
HOGENOMiHOG000281564.
KOiK00658.
OMAiKACCHAL.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR02927. SucB_Actino. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NNJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSVEMPEL GESVTEGTIT QWLKSVGDTV EVDEPLLEVS TDKVDTEIPS
60 70 80 90 100
PVAGVILEIK AEEDDTVDVG GVIAIIGDAD ETPANEAPAD EAPAPAEEEE
110 120 130 140 150
PVKEEPKKEA APEAPAATGA ATDVEMPELG ESVTEGTITQ WLKAVGDTVE
160 170 180 190 200
VDEPLLEVST DKVDTEIPSP VAGTIVEILA DEDDTVDVGA VIARIGDANA
210 220 230 240 250
AAAPAEEEAA PAEEEEPVKE EPKKEAAPEA PAATGAATDV EMPELGESVT
260 270 280 290 300
EGTITQWLKA VGDTVEVDEP LLEVSTDKVD TEIPSPVAGT IVEILADEDD
310 320 330 340 350
TVDVGAVIAR IGDANAAAAP AEEEAAPAEE EEPVKEEPKK EEPKKEEPKK
360 370 380 390 400
EAATTPAAAS ATVSASGDNV PYVTPLVRKL AEKHGVDLNT VTGTGIGGRI
410 420 430 440 450
RKQDVLAAAN GEAAPAEAAA PVSAWSTKSV DPEKAKLRGT TQKVNRIREI
460 470 480 490 500
TAMKTVEALQ ISAQLTQLHE VDMTRVAELR KKNKPAFIEK HGVNLTYLPF
510 520 530 540 550
FVKAVVEALV SHPNVNASFN AKTKEMTYHS SVNLSIAVDT PAGLLTPVIH
560 570 580 590 600
DAQDLSIPEI AKAIVDLADR SRNNKLKPND LSGGTFTITN IGSEGALSDT
610 620 630 640 650
PILVPPQAGI LGTGAIVKRP VVITEDGIDS IAIRQMVFLP LTYDHQVVDG
660 670
ADAGRFLTTI KDRLETANFE GDLQL
Length:675
Mass (Da):70,905
Last modified:October 1, 2002 - v1
Checksum:i1D262FA89899B47F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB99600.1.
BX927154 Genomic DNA. Translation: CAF20547.1.
RefSeqiNP_601410.1. NC_003450.3.
WP_011014958.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99600; BAB99600; BAB99600.
CAF20547; CAF20547; cg2421.
GeneIDi1020158.
KEGGicgb:cg2421.
cgl:NCgl2126.
PATRICi21496412. VBICorGlu203724_2142.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000036 Genomic DNA. Translation: BAB99600.1.
BX927154 Genomic DNA. Translation: CAF20547.1.
RefSeqiNP_601410.1. NC_003450.3.
WP_011014958.1. NC_006958.1.

3D structure databases

ProteinModelPortaliQ8NNJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2421.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99600; BAB99600; BAB99600.
CAF20547; CAF20547; cg2421.
GeneIDi1020158.
KEGGicgb:cg2421.
cgl:NCgl2126.
PATRICi21496412. VBICorGlu203724_2142.

Phylogenomic databases

eggNOGiCOG0508. LUCA.
HOGENOMiHOG000281564.
KOiK00658.
OMAiKACCHAL.

Enzyme and pathway databases

BioCyciCGLU1204414:G134W-2125-MONOMER.
CORYNE:G18NG-11799-MONOMER.
BRENDAi2.3.1.61. 960.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR02927. SucB_Actino. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODP2_CORGL
AccessioniPrimary (citable) accession number: Q8NNJ2
Secondary accession number(s): Q6M3N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Is the only lipoylated protein in C.glutamicum.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.