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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)DescriptionActionsGraphical viewLength
Binding sitei29Thiamine pyrophosphate1 Publication1
Binding sitei82Thiamine pyrophosphate1 Publication1
Active sitei129Proton acceptorCurated1
Binding sitei129SubstrateCurated1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-238-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)DescriptionActionsGraphical viewLength
ChainiPRO_00002949771 – 3242-oxoisovalerate dehydrogenase subunit betaAdd BLAST324

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 interactor.
STRINGi300852.TTHA0230.

Structurei

Secondary structure

1324
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 20Combined sources15
Beta strandi24 – 28Combined sources5
Turni40 – 43Combined sources4
Helixi44 – 48Combined sources5
Turni50 – 52Combined sources3
Beta strandi53 – 55Combined sources3
Helixi60 – 73Combined sources14
Beta strandi76 – 80Combined sources5
Helixi84 – 86Combined sources3
Helixi88 – 90Combined sources3
Helixi91 – 96Combined sources6
Turni97 – 100Combined sources4
Helixi101 – 104Combined sources4
Turni105 – 107Combined sources3
Beta strandi114 – 119Combined sources6
Beta strandi121 – 124Combined sources4
Helixi126 – 128Combined sources3
Helixi134 – 138Combined sources5
Beta strandi144 – 147Combined sources4
Helixi151 – 163Combined sources13
Beta strandi168 – 173Combined sources6
Helixi174 – 176Combined sources3
Beta strandi177 – 179Combined sources3
Beta strandi197 – 200Combined sources4
Beta strandi203 – 209Combined sources7
Helixi211 – 213Combined sources3
Helixi214 – 226Combined sources13
Beta strandi231 – 235Combined sources5
Beta strandi238 – 240Combined sources3
Helixi244 – 254Combined sources11
Beta strandi257 – 265Combined sources9
Helixi269 – 281Combined sources13
Helixi282 – 284Combined sources3
Beta strandi290 – 294Combined sources5
Helixi304 – 307Combined sources4
Helixi311 – 323Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLR3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni58 – 60Thiamine pyrophosphate binding3
Regioni83 – 86Substrate binding4
Regioni86 – 89Thiamine pyrophosphate binding4

Phylogenomic databases

eggNOGiENOG4105CPP. Bacteria.
COG0022. LUCA.
HOGENOMiHOG000281451.
KOiK00167.
OMAiFPAMEHL.
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)DescriptionActionsGraphical viewLength
Sequence conflicti209G → C (PubMed:15033367).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5SLR3. 1 interactor.
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.
PhylomeDBiQ5SLR3.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-238-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...

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: November 2, 2016
This is version 76 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.