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P10802

- ODP2_AZOVI

UniProt

P10802 - ODP2_AZOVI

Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene
N/A
Organism
Azotobacter vinelandii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (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 3 lipoyl cofactors covalently.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei611 – 6111Sequence 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
    OrganismiAzotobacter vinelandii
    Taxonomic identifieri354 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

    Subcellular locationi

    GO - Cellular componenti

    1. pyruvate dehydrogenase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 638637Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexPRO_0000162272Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401N6-lipoyllysineSequence Analysis
    Modified residuei157 – 1571N6-lipoyllysineSequence Analysis
    Modified residuei262 – 2621N6-lipoyllysineSequence Analysis

    Interactioni

    Subunit structurei

    Forms a 24-polypeptide structural core with octahedral symmetry.

    Structurei

    Secondary structure

    1
    638
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi11 – 199
    Beta strandi29 – 379
    Beta strandi42 – 465
    Beta strandi48 – 5710
    Beta strandi63 – 653
    Beta strandi68 – 747
    Helixi404 – 4063
    Helixi417 – 43216
    Beta strandi435 – 4439
    Helixi445 – 4539
    Helixi455 – 4606
    Helixi468 – 48114
    Helixi483 – 4864
    Beta strandi487 – 4893
    Beta strandi496 – 4983
    Beta strandi504 – 5063
    Beta strandi508 – 5103
    Beta strandi513 – 5153
    Beta strandi518 – 5203
    Helixi522 – 5243
    Helixi527 – 54216
    Helixi548 – 5514
    Beta strandi555 – 5606
    Turni562 – 5643
    Beta strandi577 – 5837
    Beta strandi587 – 5926
    Beta strandi594 – 61017
    Turni611 – 6133
    Helixi616 – 63116
    Helixi633 – 6375

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DPBX-ray2.50A396-638[»]
    1DPCX-ray2.60A396-638[»]
    1DPDX-ray2.70A396-638[»]
    1EAAX-ray2.60A396-638[»]
    1EABX-ray2.60A396-638[»]
    1EACX-ray2.60A396-638[»]
    1EADX-ray2.60A396-638[»]
    1EAEX-ray2.60A396-638[»]
    1EAFX-ray2.60A396-638[»]
    1IYUNMR-A2-79[»]
    1IYVNMR-A2-79[»]
    ProteinModelPortaliP10802.
    SMRiP10802. Positions 2-79, 396-638.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10802.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7372Lipoyl-binding 1Add
    BLAST
    Domaini118 – 19073Lipoyl-binding 2Add
    BLAST
    Domaini223 – 29573Lipoyl-binding 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni328 – 38154E1/E3 bindingAdd
    BLAST
    Regioni382 – 638257CatalyticAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Lipoyl, Repeat

    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.
    IPR006256. AcTrfase_Pyrv_DH_cplx.
    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.
    TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10802-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEIIRVPDI GGDGEVIELL VKTGDLIEVE QGLVVLESAK ASMEVPSPKA    50
    GVVKSVSVKL GDKLKEGDAI IELEPAAGAA AAPAEAAAVP AAPTQAVDEA 100
    EAPSPGASAT PAPAAASQEV RVPDIGSAGK ARVIEVLVKA GDQVQAEQSL 150
    IVLESDKASM EIPSPASGVV ESVAIQLNAE VGTGDLILTL RTTGAQAQPT 200
    APAAAAAASP APAPLAPAAA GPQEVKVPDI GSAGKARVIE VLVKAGDQVQ 250
    AEQSLIVLES DKASMEIPSP AAGVVESVAV QLNAEVGTGD QILTLRVAGA 300
    APSGPRARGS PGQAAAAPGA APAPAPVGAP SRNGAKVHAG PAVRQLAREF 350
    GVELAAINST GPRGRILKED VQAYVKAMMQ KAKEAPAAGA ASGAGIPPIP 400
    PVDFAKYGEI EEVPMTRLMQ IGATNLHRSW LNVPHVTQFE SADITELEAF 450
    RVAQKAVAEK AGVKLTVLPL LLKACAYLLK ELPDFNSSLA PSGQALIRKK 500
    YVHIGFAVDT PDGLLVPVIR NVDQKSLLQL AAEAAELAEK ARSKKLGADA 550
    MQGACFTISS LGHIGGTAFT PIVNAPEVAI LGVSKASMQP VWDGKAFQPR 600
    LMLPLSLSYD HRVINGAAAA RFTKRLGDLL ADIRAILL 638
    Length:638
    Mass (Da):65,045
    Last modified:January 23, 2007 - v3
    Checksum:i8B92CB5ADEA0BEA1
    GO

    Sequence cautioni

    The sequence CAA30987.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12455 Genomic DNA. Translation: CAA30987.1. Different initiation.
    PIRiS01017. XXAV.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12455 Genomic DNA. Translation: CAA30987.1 . Different initiation.
    PIRi S01017. XXAV.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DPB X-ray 2.50 A 396-638 [» ]
    1DPC X-ray 2.60 A 396-638 [» ]
    1DPD X-ray 2.70 A 396-638 [» ]
    1EAA X-ray 2.60 A 396-638 [» ]
    1EAB X-ray 2.60 A 396-638 [» ]
    1EAC X-ray 2.60 A 396-638 [» ]
    1EAD X-ray 2.60 A 396-638 [» ]
    1EAE X-ray 2.60 A 396-638 [» ]
    1EAF X-ray 2.60 A 396-638 [» ]
    1IYU NMR - A 2-79 [» ]
    1IYV NMR - A 2-79 [» ]
    ProteinModelPortali P10802.
    SMRi P10802. Positions 2-79, 396-638.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P10802.

    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.
    IPR006256. AcTrfase_Pyrv_DH_cplx.
    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 TIGR01348. PDHac_trf_long. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
    PS00189. LIPOYL. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Molecular cloning and sequence analysis."
      Hanemaaijer R., Janssen A., de Kok A., Veeger C.
      Eur. J. Biochem. 174:593-599(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617.
    2. "The domain structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
      Hanemaaijer R., de Kok A., Jolles J., Veeger C.
      Eur. J. Biochem. 169:245-252(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16 AND 381-416.
    3. "Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2-oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy."
      Hanemaaijer R., Vervoort J., Westphal A.H., de Kok A., Veeger C.
      FEBS Lett. 240:205-210(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIPOYL DOMAIN CONFORMATION.
    4. "Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex."
      Mattevi A., Obmolova G., Schulze E., Kalk K.H., Westphal A.H., de Kok A., Hol W.G.J.
      Science 255:1544-1550(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 382-638.
    5. "Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
      Berg A., de Kok A., Vervoort J.
      Eur. J. Biochem. 221:87-100(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-79.
    6. "Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii."
      Berg A., Vervoort J., de Kok A.
      Eur. J. Biochem. 244:352-360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-79.

    Entry informationi

    Entry nameiODP2_AZOVI
    AccessioniPrimary (citable) accession number: P10802
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 112 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