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Q5SLR4

- ODBA_THET8

UniProt

Q5SLR4 - ODBA_THET8

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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

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 diphosphate1 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
Complete GO annotation...

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 – 6026Combined sources
Helixi74 – 8310Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 924Combined sources
Turni95 – 973Combined sources
Helixi98 – 1047Combined sources
Helixi108 – 1169Combined sources
Turni122 – 1254Combined sources
Turni135 – 1384Combined sources
Turni146 – 1494Combined sources
Helixi150 – 16213Combined sources
Beta strandi169 – 1746Combined sources
Helixi176 – 1794Combined sources
Helixi181 – 19212Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi205 – 2073Combined sources
Helixi212 – 2154Combined sources
Beta strandi217 – 2193Combined sources
Helixi222 – 2276Combined sources
Beta strandi232 – 2365Combined sources
Helixi240 – 25516Combined sources
Beta strandi261 – 2666Combined sources
Helixi279 – 2813Combined sources
Helixi285 – 2928Combined sources
Helixi296 – 30510Combined sources
Turni306 – 3083Combined sources
Helixi312 – 33524Combined sources
Helixi341 – 3455Combined sources
Beta strandi348 – 3514Combined sources
Helixi354 – 36613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MVKETHRFET FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM
60 70 80 90 100
LDERYTILIR TGKTSFIAPA AGHEAAQVAI AHAIRPGFDW VFPYYRDHGL
110 120 130 140 150
ALALGIPLKE LLGQMLATKA DPNKGRQMPE HPGSKALNFF TVASPIASHV
160 170 180 190 200
PPAAGAAISM KLLRTGQVAV CTFGDGATSE GDWYAGINFA AVQGAPAVFI
210 220 230 240 250
AENNFYAISV DYRHQTHSPT IADKAHAFGI PGYLVDGMDV LASYYVVKEA
260 270 280 290 300
VERARRGEGP SLVELRVYRY GPHSSADDDS RYRPKEEVAF WRKKDPIPRF
310 320 330 340 350
RRFLEARGLW NEEWEEDVRE EIRAELERGL KEAEEAGPVP PEWMFEDVFA
360
EKPWHLLRQE ALLKEEL
Length:367
Mass (Da):41,452
Last modified:December 21, 2004 - v1
Checksum:i178B4EFE0CA5F1D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70052.1 .
RefSeqi YP_143495.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 68 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