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Q5SLR4

- ODBA_THET8

UniProt

Q5SLR4 - ODBA_THET8

Protein

2-oxoisovalerate dehydrogenase subunit alpha

Gene

TTHA0229

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.By similarity

    Catalytic activityi

    3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.1 Publication

    Cofactori

    Thiamine pyrophosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei66 – 661Substrate1 Publication
    Binding sitei95 – 951Substrate1 Publication
    Binding sitei144 – 1441Substrate1 Publication
    Metal bindingi175 – 1751Magnesium1 Publication
    Metal bindingi204 – 2041Magnesium1 Publication
    Metal bindingi206 – 2061Magnesium; via carbonyl oxygen1 Publication
    Binding sitei273 – 2731Thiamine pyrophosphate1 Publication

    GO - Molecular functioni

    1. 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-238-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-oxoisovalerate dehydrogenase subunit alpha (EC:1.2.4.4)
    Alternative name(s):
    Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
    Short name:
    BCKDH E1-alpha
    Gene namesi
    Ordered Locus Names:TTHA0229
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3673672-oxoisovalerate dehydrogenase subunit alphaPRO_0000294975Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TTHA0230Q5SLR34EBI-1038222,EBI-1038230

    Protein-protein interaction databases

    IntActiQ5SLR4. 1 interaction.
    STRINGi300852.TTHA0229.

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 6026
    Helixi74 – 8310
    Turni86 – 883
    Beta strandi89 – 924
    Turni95 – 973
    Helixi98 – 1047
    Helixi108 – 1169
    Turni122 – 1254
    Turni135 – 1384
    Turni146 – 1494
    Helixi150 – 16213
    Beta strandi169 – 1746
    Helixi176 – 1794
    Helixi181 – 19212
    Beta strandi196 – 2038
    Beta strandi205 – 2073
    Helixi212 – 2154
    Beta strandi217 – 2193
    Helixi222 – 2276
    Beta strandi232 – 2365
    Helixi240 – 25516
    Beta strandi261 – 2666
    Helixi279 – 2813
    Helixi285 – 2928
    Helixi296 – 30510
    Turni306 – 3083
    Helixi312 – 33524
    Helixi341 – 3455
    Beta strandi348 – 3514
    Helixi354 – 36613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UM9X-ray2.20A/C1-367[»]
    1UMBX-ray2.10A/C1-367[»]
    1UMCX-ray2.40A/C1-367[»]
    1UMDX-ray1.90A/C1-367[»]
    ProteinModelPortaliQ5SLR4.
    SMRiQ5SLR4. Positions 6-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SLR4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 963Thiamine pyrophosphate binding1 Publication
    Regioni128 – 1314Substrate binding1 Publication
    Regioni144 – 1463Thiamine pyrophosphate binding1 Publication
    Regioni174 – 1807Thiamine pyrophosphate binding1 Publication
    Regioni204 – 2085Thiamine pyrophosphate binding1 Publication

    Sequence similaritiesi

    Belongs to the BCKDHA family.Curated

    Phylogenomic databases

    eggNOGiCOG1071.
    HOGENOMiHOG000281335.
    KOiK00166.
    OMAiNEEWEED.
    OrthoDBiEOG6VMTKR.
    PhylomeDBiQ5SLR4.

    Family and domain databases

    Gene3Di3.40.50.970. 1 hit.
    InterProiIPR001017. DH_E1.
    IPR029061. THDP-binding.
    [Graphical view]
    PfamiPF00676. E1_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q5SLR4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKETHRFET FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM    50
    LDERYTILIR TGKTSFIAPA AGHEAAQVAI AHAIRPGFDW VFPYYRDHGL 100
    ALALGIPLKE LLGQMLATKA DPNKGRQMPE HPGSKALNFF TVASPIASHV 150
    PPAAGAAISM KLLRTGQVAV CTFGDGATSE GDWYAGINFA AVQGAPAVFI 200
    AENNFYAISV DYRHQTHSPT IADKAHAFGI PGYLVDGMDV LASYYVVKEA 250
    VERARRGEGP SLVELRVYRY GPHSSADDDS RYRPKEEVAF WRKKDPIPRF 300
    RRFLEARGLW NEEWEEDVRE EIRAELERGL KEAEEAGPVP PEWMFEDVFA 350
    EKPWHLLRQE ALLKEEL 367
    Length:367
    Mass (Da):41,452
    Last modified:December 21, 2004 - v1
    Checksum:i178B4EFE0CA5F1D1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD70052.1.
    RefSeqiYP_143495.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD70052; BAD70052; BAD70052.
    GeneIDi3168003.
    KEGGittj:TTHA0229.
    PATRICi23955399. VBITheThe93045_0227.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008226 Genomic DNA. Translation: BAD70052.1 .
    RefSeqi YP_143495.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UM9 X-ray 2.20 A/C 1-367 [» ]
    1UMB X-ray 2.10 A/C 1-367 [» ]
    1UMC X-ray 2.40 A/C 1-367 [» ]
    1UMD X-ray 1.90 A/C 1-367 [» ]
    ProteinModelPortali Q5SLR4.
    SMRi Q5SLR4. Positions 6-367.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q5SLR4. 1 interaction.
    STRINGi 300852.TTHA0229.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD70052 ; BAD70052 ; BAD70052 .
    GeneIDi 3168003.
    KEGGi ttj:TTHA0229.
    PATRICi 23955399. VBITheThe93045_0227.

    Phylogenomic databases

    eggNOGi COG1071.
    HOGENOMi HOG000281335.
    KOi K00166.
    OMAi NEEWEED.
    OrthoDBi EOG6VMTKR.
    PhylomeDBi Q5SLR4.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-238-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5SLR4.

    Family and domain databases

    Gene3Di 3.40.50.970. 1 hit.
    InterProi IPR001017. DH_E1.
    IPR029061. THDP-binding.
    [Graphical view ]
    Pfami PF00676. E1_dh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    2. "Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography."
      Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., Kamiya N.
      J. Mol. Biol. 337:1011-1033(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ODBB AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiODBA_THET8
    AccessioniPrimary (citable) accession number: Q5SLR4
    Secondary accession number(s): P84129
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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