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Q8NNJ2

- ODP2_CORGL

UniProt

Q8NNJ2 - ODP2_CORGL

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: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    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

    Binds 3 lipoyl cofactors covalently.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei645 – 6451By similarity
    Active sitei649 – 6491By similarity

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW
    2. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis, Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciCGLU1204414-WGS:GSME-2125-MONOMER.

    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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
    ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431K → Q: No effect on ODH and PDH activity; when associated with Q-162. 1 Publication
    Mutagenesisi162 – 1621K → 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 Publication
    Mutagenesisi278 – 2781K → Q: Strong reduction in the catalytic efficiency of ODH and slight reduction in that of PDH; when associated with Q-162. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 675675Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000420521Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysine1 Publication
    Modified residuei162 – 1621N6-lipoyllysine1 Publication
    Modified residuei278 – 2781N6-lipoyllysine1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7674Lipoyl-binding 1Add
    BLAST
    Domaini122 – 19574Lipoyl-binding 2Add
    BLAST
    Domaini238 – 31174Lipoyl-binding 3Add
    BLAST
    Domaini371 – 40737E3-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi81 – 351271Glu-richAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl, Repeat

    Phylogenomic databases

    HOGENOMiHOG000281564.
    KOiK00658.
    OMAiPDDTQGG.
    OrthoDBiEOG610413.

    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

    MAFSVEMPEL GESVTEGTIT QWLKSVGDTV EVDEPLLEVS TDKVDTEIPS    50
    PVAGVILEIK AEEDDTVDVG GVIAIIGDAD ETPANEAPAD EAPAPAEEEE 100
    PVKEEPKKEA APEAPAATGA ATDVEMPELG ESVTEGTITQ WLKAVGDTVE 150
    VDEPLLEVST DKVDTEIPSP VAGTIVEILA DEDDTVDVGA VIARIGDANA 200
    AAAPAEEEAA PAEEEEPVKE EPKKEAAPEA PAATGAATDV EMPELGESVT 250
    EGTITQWLKA VGDTVEVDEP LLEVSTDKVD TEIPSPVAGT IVEILADEDD 300
    TVDVGAVIAR IGDANAAAAP AEEEAAPAEE EEPVKEEPKK EEPKKEEPKK 350
    EAATTPAAAS ATVSASGDNV PYVTPLVRKL AEKHGVDLNT VTGTGIGGRI 400
    RKQDVLAAAN GEAAPAEAAA PVSAWSTKSV DPEKAKLRGT TQKVNRIREI 450
    TAMKTVEALQ ISAQLTQLHE VDMTRVAELR KKNKPAFIEK HGVNLTYLPF 500
    FVKAVVEALV SHPNVNASFN AKTKEMTYHS SVNLSIAVDT PAGLLTPVIH 550
    DAQDLSIPEI AKAIVDLADR SRNNKLKPND LSGGTFTITN IGSEGALSDT 600
    PILVPPQAGI LGTGAIVKRP VVITEDGIDS IAIRQMVFLP LTYDHQVVDG 650
    ADAGRFLTTI KDRLETANFE GDLQL 675
    Length:675
    Mass (Da):70,905
    Last modified:October 1, 2002 - v1
    Checksum:i1D262FA89899B47F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB99600.1.
    BX927154 Genomic DNA. Translation: CAF20547.1.
    RefSeqiNP_601410.1. NC_003450.3.
    YP_226448.1. 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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000036 Genomic DNA. Translation: BAB99600.1 .
    BX927154 Genomic DNA. Translation: CAF20547.1 .
    RefSeqi NP_601410.1. NC_003450.3.
    YP_226448.1. NC_006958.1.

    3D structure databases

    ProteinModelPortali Q8NNJ2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 196627.cg2421.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB99600 ; BAB99600 ; BAB99600 .
    CAF20547 ; CAF20547 ; cg2421 .
    GeneIDi 1020158.
    KEGGi cgb:cg2421.
    cgl:NCgl2126.
    PATRICi 21496412. VBICorGlu203724_2142.

    Phylogenomic databases

    HOGENOMi HOG000281564.
    KOi K00658.
    OMAi PDDTQGG.
    OrthoDBi EOG610413.

    Enzyme and pathway databases

    BioCyci CGLU1204414-WGS:GSME-2125-MONOMER.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 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 ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 3 hits.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 3 hits.
    TIGRFAMsi TIGR02927. SucB_Actino. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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 AT LYS-43; LYS-162 AND LYS-278, MUTAGENESIS OF LYS-43; LYS-162 AND LYS-278.
      Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

    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: October 1, 2014
    This is version 96 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

    External Data

    Dasty 3