Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2T7H6 (LEU3_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydrogenase

EC=1.1.1.85
Alternative name(s):
3-IPM-DH
Beta-IPM dehydrogenase
Short name=IMDH
Gene names
Name:leuB
Ordered Locus Names:BTH_II0674
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate By similarity. HAMAP-Rule MF_01033

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. HAMAP-Rule MF_01033

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. HAMAP-Rule MF_01033

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01033

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01033.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3553553-isopropylmalate dehydrogenase HAMAP-Rule MF_01033
PRO_0000250109

Regions

Nucleotide binding280 – 29213NAD By similarity

Sites

Metal binding2221Magnesium or manganese By similarity
Metal binding2461Magnesium or manganese By similarity
Metal binding2501Magnesium or manganese By similarity
Binding site901Substrate By similarity
Binding site1001Substrate By similarity
Binding site1281Substrate By similarity
Binding site2221Substrate By similarity
Site1351Important for catalysis By similarity
Site1901Important for catalysis By similarity

Secondary structure

.................................................................... 355
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2T7H6 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: CE8C13AF0007C5E4

FASTA35538,242
        10         20         30         40         50         60 
MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEHAPVGGA GYEASGHPLP DATLALAKEA 

        70         80         90        100        110        120 
DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR PAICYPQLVD ASPLKPELVA 

       130        140        150        160        170        180 
GLDILIVREL NGDIYFGQPR GVRAAPDGPF AGEREGFDTM RYSEPEVRRI AHVAFQAAQK 

       190        200        210        220        230        240 
RAKKLLSVDK SNVLETSQFW RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT 

       250        260        270        280        290        300 
GNMFGDILSD EASMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGI ANPLATILSA 

       310        320        330        340        350 
AMLLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGCR QVGTAAMGDA VVAAL 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000085 Genomic DNA. Translation: ABC35976.1.
RefSeqYP_438873.1. NC_007650.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IWHX-ray1.75A/B1-355[»]
ProteinModelPortalQ2T7H6.
SMRQ2T7H6. Positions 2-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_II0674.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC35976; ABC35976; BTH_II0674.
GeneID3845853.
KEGGbte:BTH_II0674.
PATRIC19298864. VBIBurTha36512_0762.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0473.
HOGENOMHOG000021112.
KOK00052.
OMAAKSTVEM.
OrthoDBEOG65N1BN.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-4018-MONOMER.
UniPathwayUPA00048; UER00072.

Family and domain databases

Gene3D3.40.718.10. 1 hit.
HAMAPMF_01033. LeuB_type1.
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
PANTHERPTHR11835. PTHR11835. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. leuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU3_BURTA
AccessionPrimary (citable) accession number: Q2T7H6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways