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Protein

2-oxoisovalerate dehydrogenase subunit alpha

Gene

bkdA1

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
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).

Catalytic activityi

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

Cofactori

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6666-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
Name:bkdA1
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4104102-oxoisovalerate dehydrogenase subunit alphaPRO_0000162249Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

DIPiDIP-6208N.
IntActiP09060. 1 interaction.
MINTiMINT-100326.
STRINGi160488.PP_4401.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi44 – 474Combined sources
Helixi48 – 514Combined sources
Helixi67 – 693Combined sources
Helixi74 – 9926Combined sources
Beta strandi102 – 1043Combined sources
Turni110 – 1123Combined sources
Helixi113 – 12210Combined sources
Beta strandi127 – 1304Combined sources
Helixi136 – 1416Combined sources
Helixi146 – 1549Combined sources
Turni160 – 1634Combined sources
Helixi173 – 1753Combined sources
Beta strandi182 – 1854Combined sources
Helixi186 – 20015Combined sources
Beta strandi207 – 2126Combined sources
Helixi214 – 2174Combined sources
Helixi219 – 23113Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi243 – 2453Combined sources
Helixi250 – 2534Combined sources
Turni254 – 2574Combined sources
Helixi262 – 2665Combined sources
Beta strandi270 – 2756Combined sources
Helixi279 – 29416Combined sources
Beta strandi300 – 3056Combined sources
Helixi318 – 3203Combined sources
Helixi326 – 3294Combined sources
Helixi335 – 34511Combined sources
Helixi351 – 37323Combined sources
Beta strandi378 – 3803Combined sources
Helixi388 – 3903Combined sources
Beta strandi391 – 3966Combined sources
Helixi399 – 4068Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QS0X-ray2.40A2-408[»]
2BP7X-ray2.90A/C/E/G1-410[»]
ProteinModelPortaliP09060.
SMRiP09060. Positions 2-408.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09060.

Family & Domainsi

Sequence similaritiesi

Belongs to the BCKDHA family.Curated

Phylogenomic databases

eggNOGiENOG4107R0V. Bacteria.
COG1071. LUCA.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR022593. Oxoisoval_DH_suAlpha_N_dom.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
PF12573. OxoDH_E1alpha_N. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.

Sequencei

Sequence statusi: Complete.

P09060-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEYAPLRLH VPEPTGRPGC QTDFSYLRLN DAGQARKPPV DVDAADTADL
60 70 80 90 100
SYSLVRVLDE QGDAQGPWAE DIDPQILRQG MRAMLKTRIF DSRMVVAQRQ
110 120 130 140 150
KKMSFYMQSL GEEAIGSGQA LALNRTDMCF PTYRQQSILM ARDVSLVEMI
160 170 180 190 200
CQLLSNERDP LKGRQLPIMY SVREAGFFTI SGNLATQFVQ AVGWAMASAI
210 220 230 240 250
KGDTKIASAW IGDGATAESD FHTALTFAHV YRAPVILNVV NNQWAISTFQ
260 270 280 290 300
AIAGGESTTF AGRGVGCGIA SLRVDGNDFV AVYAASRWAA ERARRGLGPS
310 320 330 340 350
LIEWVTYRAG PHSTSDDPSK YRPADDWSHF PLGDPIARLK QHLIKIGHWS
360 370 380 390 400
EEEHQATTAE FEAAVIAAQK EAEQYGTLAN GHIPSAASMF EDVYKEMPDH
410
LRRQRQELGV
Length:410
Mass (Da):45,268
Last modified:February 1, 1996 - v2
Checksum:i0C998460CCFB9CF4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57613 Genomic DNA. Translation: AAA65614.1.
PIRiS01317. DEPSXA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57613 Genomic DNA. Translation: AAA65614.1.
PIRiS01317. DEPSXA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QS0X-ray2.40A2-408[»]
2BP7X-ray2.90A/C/E/G1-410[»]
ProteinModelPortaliP09060.
SMRiP09060. Positions 2-408.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6208N.
IntActiP09060. 1 interaction.
MINTiMINT-100326.
STRINGi160488.PP_4401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107R0V. Bacteria.
COG1071. LUCA.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6666-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP09060.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR022593. Oxoisoval_DH_suAlpha_N_dom.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
PF12573. OxoDH_E1alpha_N. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Similarity of the E1 subunits of branched-chain-oxoacid dehydrogenase from Pseudomonas putida to the corresponding subunits of mammalian branched-chain-oxoacid and pyruvate dehydrogenases."
    Burns G., Brown T., Hatter K., Idriss J., Sokatch J.R.
    Eur. J. Biochem. 176:311-317(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G2.
  2. "Transcriptional analysis of the promoter region of the Pseudomonas putida branched-chain keto acid dehydrogenase operon."
    Madhusudhan K.T., Huang G., Burns G., Sokatch J.R.
    J. Bacteriol. 172:5655-5663(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
    Strain: G2.
  3. "Purification of active E1 alpha 2 beta 2 of Pseudomonas putida branched-chain-oxoacid dehydrogenase."
    Hester K., Luo J., Burns G., Braswell E.H., Sokatch J.R.
    Eur. J. Biochem. 233:828-836(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-13.
  4. "Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes."
    Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G.J.
    Nat. Struct. Biol. 6:785-792(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Entry informationi

Entry nameiODBA_PSEPU
AccessioniPrimary (citable) accession number: P09060
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1996
Last modified: November 11, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.