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Protein

2-oxoisovalerate dehydrogenase subunit alpha

Gene

TT_C1757

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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.By similarity

Cofactori

thiamine diphosphateBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661SubstrateBy similarity
Binding sitei95 – 951SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Metal bindingi175 – 1751MagnesiumBy similarity
Metal bindingi204 – 2041MagnesiumBy similarity
Metal bindingi206 – 2061Magnesium; via carbonyl oxygenBy similarity
Binding sitei273 – 2731Thiamine pyrophosphateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciTTHE262724:GCAT-1795-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:TT_C1757
OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Taxonomic identifieri262724 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000592 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3673672-oxoisovalerate dehydrogenase subunit alphaPRO_0000294974Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex (By similarity).By similarity

Protein-protein interaction databases

STRINGi262724.TTC1757.

Structurei

3D structure databases

ProteinModelPortaliQ72GU1.
SMRiQ72GU1. Positions 6-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the BCKDHA family.Curated

Phylogenomic databases

eggNOGiCOG1071.
KOiK00166.
OMAiCYGNADD.
OrthoDBiEOG6VMTKR.

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.

Q72GU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKETHRFEP FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM
60 70 80 90 100
LDERYTILIR TGKTSFIAPA AGHEAAQVAI AHAIRPGFDW VFPYYRDHGL
110 120 130 140 150
ALALGIPLKE LFGQMLATKA DPNKGRQMPE HPGSKALNFF TVASPIASHV
160 170 180 190 200
PPAAGAAISM KLLRTGQVAV CTFGDGATSE GDWYAGINFA AVQGAPAVFV
210 220 230 240 250
CENNFYAISV DYRHQTHSPT IADKAHAFGI PGYLVDGMDV LASYYVVKEA
260 270 280 290 300
VERARRGEGP SLVELRVYRY GPHSSADDDS RYRPKEEVAF WRKKDPIPRF
310 320 330 340 350
RRFLEARGLW NEEWEEDVRE EIRAELERGL KEAEEAGPVP PEWMFADVFA
360
EKPWHLLRQE ALLKEEL
Length:367
Mass (Da):41,442
Last modified:July 5, 2004 - v1
Checksum:i726F33C315656E49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017221 Genomic DNA. Translation: AAS82099.1.
RefSeqiWP_011174115.1. NC_005835.1.

Genome annotation databases

EnsemblBacteriaiAAS82099; AAS82099; TT_C1757.
KEGGitth:TTC1757.
PATRICi23953983. VBITheThe54392_1757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017221 Genomic DNA. Translation: AAS82099.1.
RefSeqiWP_011174115.1. NC_005835.1.

3D structure databases

ProteinModelPortaliQ72GU1.
SMRiQ72GU1. Positions 6-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS82099; AAS82099; TT_C1757.
KEGGitth:TTC1757.
PATRICi23953983. VBITheThe54392_1757.

Phylogenomic databases

eggNOGiCOG1071.
KOiK00166.
OMAiCYGNADD.
OrthoDBiEOG6VMTKR.

Enzyme and pathway databases

BioCyciTTHE262724:GCAT-1795-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB27 / ATCC BAA-163 / DSM 7039.

Entry informationi

Entry nameiODBA_THET2
AccessioniPrimary (citable) accession number: Q72GU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 67 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.