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Protein

2-oxoisovalerate dehydrogenase subunit beta

Gene

TTHA0230

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 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.Curated1 Publication

Cofactori

thiamine diphosphateCurated1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Thiamine pyrophosphate1 Publication
Binding sitei82 – 821Thiamine pyrophosphate1 Publication
Active sitei129 – 1291Proton acceptorCurated
Binding sitei129 – 1291SubstrateCurated

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-239-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoisovalerate dehydrogenase subunit beta (EC:1.2.4.4)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
Short name:
BCKDH E1-beta
Gene namesi
Ordered Locus Names:TTHA0230
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3243242-oxoisovalerate dehydrogenase subunit betaPRO_0000294977Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains. Directly associated with ODBA in the E1 complex.Curated1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TTHA0229Q5SLR44EBI-1038230,EBI-1038222

Protein-protein interaction databases

IntActiQ5SLR3. 1 interaction.
STRINGi300852.TTHA0230.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2015Combined sources
Beta strandi24 – 285Combined sources
Turni40 – 434Combined sources
Helixi44 – 485Combined sources
Turni50 – 523Combined sources
Beta strandi53 – 553Combined sources
Helixi60 – 7314Combined sources
Beta strandi76 – 805Combined sources
Helixi84 – 863Combined sources
Helixi88 – 903Combined sources
Helixi91 – 966Combined sources
Turni97 – 1004Combined sources
Helixi101 – 1044Combined sources
Turni105 – 1073Combined sources
Beta strandi114 – 1196Combined sources
Beta strandi121 – 1244Combined sources
Helixi126 – 1283Combined sources
Helixi134 – 1385Combined sources
Beta strandi144 – 1474Combined sources
Helixi151 – 16313Combined sources
Beta strandi168 – 1736Combined sources
Helixi174 – 1763Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi203 – 2097Combined sources
Helixi211 – 2133Combined sources
Helixi214 – 22613Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi238 – 2403Combined sources
Helixi244 – 25411Combined sources
Beta strandi257 – 2659Combined sources
Helixi269 – 28113Combined sources
Helixi282 – 2843Combined sources
Beta strandi290 – 2945Combined sources
Helixi304 – 3074Combined sources
Helixi311 – 32313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM9X-ray2.20B/D1-324[»]
1UMBX-ray2.10B/D1-324[»]
1UMCX-ray2.40B/D1-324[»]
1UMDX-ray1.90B/D1-324[»]
ProteinModelPortaliQ5SLR3.
SMRiQ5SLR3. Positions 2-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLR3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 603Thiamine pyrophosphate binding
Regioni83 – 864Substrate binding
Regioni86 – 894Thiamine pyrophosphate binding

Phylogenomic databases

eggNOGiENOG4105CPP. Bacteria.
COG0022. LUCA.
HOGENOMiHOG000281451.
KOiK00167.
OMAiFPAMEHL.
OrthoDBiEOG6JQH4C.
PhylomeDBiQ5SLR3.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5SLR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALMTMVQAL NRALDEEMAK DPRVVVLGED VGKRGGVFLV TEGLLQKYGP
60 70 80 90 100
DRVMDTPLSE AAIVGAALGM AAHGLRPVAE IQFADYIFPG FDQLVSQVAK
110 120 130 140 150
LRYRSGGQFT APLVVRMPSG GGVRGGHHHS QSPEAHFVHT AGLKVVAVST
160 170 180 190 200
PYDAKGLLKA AIRDEDPVVF LEPKRLYRSV KEEVPEEDYT LPIGKAALRR
210 220 230 240 250
EGKDLTLIGY GTVMPEVLQA AAELAKAGVS AEVLDLRTLM PWDYEAVMNS
260 270 280 290 300
VAKTGRVVLV SDAPRHASFV SEVAATIAED LLDMLLAPPI RVTGFDTPYP
310 320
YAQDKLYLPT VTRILNAAKR ALDY
Length:324
Mass (Da):35,093
Last modified:December 21, 2004 - v1
Checksum:i679926805496D29A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091G → C (PubMed:15033367).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70053.1.
RefSeqiWP_011227794.1. NC_006461.1.
YP_143496.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70053; BAD70053; BAD70053.
GeneIDi3168889.
KEGGittj:TTHA0230.
PATRICi23955401. VBITheThe93045_0228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70053.1.
RefSeqiWP_011227794.1. NC_006461.1.
YP_143496.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM9X-ray2.20B/D1-324[»]
1UMBX-ray2.10B/D1-324[»]
1UMCX-ray2.40B/D1-324[»]
1UMDX-ray1.90B/D1-324[»]
ProteinModelPortaliQ5SLR3.
SMRiQ5SLR3. Positions 2-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5SLR3. 1 interaction.
STRINGi300852.TTHA0230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70053; BAD70053; BAD70053.
GeneIDi3168889.
KEGGittj:TTHA0230.
PATRICi23955401. VBITheThe93045_0228.

Phylogenomic databases

eggNOGiENOG4105CPP. Bacteria.
COG0022. LUCA.
HOGENOMiHOG000281451.
KOiK00167.
OMAiFPAMEHL.
OrthoDBiEOG6JQH4C.
PhylomeDBiQ5SLR3.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-239-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLR3.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
IPR033247. Transketolase_fam.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

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 ODBA AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiODBB_THET8
AccessioniPrimary (citable) accession number: Q5SLR3
Secondary accession number(s): P84130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 73 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.