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P11961

- ODP2_GEOSE

UniProt

P11961 - ODP2_GEOSE

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

pdhC

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

    Catalytic activityi

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

    Cofactori

    Binds 1 lipoyl cofactor covalently.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei399 – 3991Sequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycolytic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Glycolysis

    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
    E2
    Gene namesi
    Name:pdhC
    OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
    Taxonomic identifieri1422 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 428427Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162273Add
    BLAST

    Amino acid modifications

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

    Interactioni

    Subunit structurei

    Forms a 60-polypeptide structural core with icosahedral symmetry.

    Protein-protein interaction databases

    DIPiDIP-6156N.
    IntActiP11961. 2 interactions.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Beta strandi16 – 216
    Beta strandi37 – 404
    Beta strandi45 – 484
    Beta strandi59 – 613
    Beta strandi63 – 675
    Beta strandi69 – 713
    Helixi133 – 1419
    Turni146 – 1483
    Helixi154 – 1563
    Helixi160 – 1678

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B5SX-ray4.40A/B/C/D/E185-426[»]
    1EBDX-ray2.60C130-170[»]
    1LABNMR-A2-81[»]
    1LACNMR-A2-81[»]
    1W3DNMR-A119-171[»]
    1W4ENMR-A126-170[»]
    1W4FNMR-A126-170[»]
    1W4GNMR-A126-170[»]
    1W85X-ray2.00I/J123-171[»]
    1W88X-ray2.30I/J123-171[»]
    2PDDNMR-A129-171[»]
    2PDENMR-A129-171[»]
    3DUFX-ray2.50I/J1-428[»]
    3DV0X-ray2.50I/J1-428[»]
    3DVAX-ray2.35I/J1-428[»]
    ProteinModelPortaliP11961.
    SMRiP11961. Positions 2-81, 126-170, 185-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11961.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7675Lipoyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 17143E1/E3 bindingAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl

    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.
    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. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11961-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFEFKLPDI GEGIHEGEIV KWFVKPGDEV NEDDVLCEVQ NDKAVVEIPS    50
    PVKGKVLEIL VPEGTVATVG QTLITLDAPG YENMTFKGQE QEEAKKEEKT 100
    ETVSKEEKVD AVAPNAPAAE AEAGPNRRVI AMPSVRKYAR EKGVDIRLVQ 150
    GTGKNGRVLK EDIDAFLAGG AKPAPAAAEE KAAPAAAKPA TTEGEFPETR 200
    EKMSGIRRAI AKAMVHSKHT APHVTLMDEA DVTKLVAHRK KFKAIAAEKG 250
    IKLTFLPYVV KALVSALREY PVLNTSIDDE TEEIIQKHYY NIGIAADTDR 300
    GLLVPVIKHA DRKPIFALAQ EINELAEKAR DGKLTPGEMK GASCTITNIG 350
    SAGGQWFTPV INHPEVAILG IGRIAEKPIV RDGEIVAAPM LALSLSFDHR 400
    MIDGATAQKA LNHIKRLLSD PELLLMEA 428
    Length:428
    Mass (Da):46,326
    Last modified:January 23, 2007 - v3
    Checksum:i2600CD150261ACB0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53560 Genomic DNA. Translation: CAA37630.1.
    PIRiS10799. S14426.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53560 Genomic DNA. Translation: CAA37630.1 .
    PIRi S10799. S14426.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B5S X-ray 4.40 A/B/C/D/E 185-426 [» ]
    1EBD X-ray 2.60 C 130-170 [» ]
    1LAB NMR - A 2-81 [» ]
    1LAC NMR - A 2-81 [» ]
    1W3D NMR - A 119-171 [» ]
    1W4E NMR - A 126-170 [» ]
    1W4F NMR - A 126-170 [» ]
    1W4G NMR - A 126-170 [» ]
    1W85 X-ray 2.00 I/J 123-171 [» ]
    1W88 X-ray 2.30 I/J 123-171 [» ]
    2PDD NMR - A 129-171 [» ]
    2PDE NMR - A 129-171 [» ]
    3DUF X-ray 2.50 I/J 1-428 [» ]
    3DV0 X-ray 2.50 I/J 1-428 [» ]
    3DVA X-ray 2.35 I/J 1-428 [» ]
    ProteinModelPortali P11961.
    SMRi P11961. Positions 2-81, 126-170, 185-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6156N.
    IntActi P11961. 2 interactions.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P11961.

    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.
    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. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of the genes encoding the alpha and beta subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
      Hawkins C.F., Borges A., Perham R.N.
      Eur. J. Biochem. 191:337-346(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924.
    2. "Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus."
      Packman L.C., Borges A., Perham R.N.
      Biochem. J. 252:79-86(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-201.
    3. "Sequence-specific 1H-NMR assignments and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex."
      Dardel F., Laue E.D., Perham R.N.
      Eur. J. Biochem. 201:203-209(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-86.
    4. "Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex."
      Dardel F., Davis A.L., Laue E.D., Perham R.N.
      J. Mol. Biol. 229:1037-1048(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-86, LIPOYLATION AT LYS-43.
    5. "The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
      Kalia Y.N., Brocklehurst S.M., Hipps D.S., Appella E., Sakaguchi K., Perham R.N.
      J. Mol. Biol. 230:323-341(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 129-171.
    6. "Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase."
      Mande S.S., Sarfaty S., Allen M.D., Perham R.N., Hol W.G.J.
      Structure 4:277-286(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 129-171.

    Entry informationi

    Entry nameiODP2_GEOSE
    AccessioniPrimary (citable) accession number: P11961
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3