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Reviewed, UniProtKB/Swiss-Prot Q56268 (LEU3_THIFE)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    3-isopropylmalate dehydrogenase
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase
      Short name=IMDH
    3-IPM-DH
Gene names
Name: leuB
OrganismThiobacillus ferrooxidans (Acidithiobacillus ferrooxidans)
Taxonomic identifier920 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus

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Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. HAMAP MF_01033

Catalytic activity

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

Cofactor

Binds 1 magnesium or ion per subunit. HAMAP MF_01033

Pathway

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

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm. HAMAP MF_01033

Sequence similarities

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3583583-isopropylmalate dehydrogenase HAMAP MF_01033
PRO_0000083777

Regions

Nucleotide binding75 – 8814NAD By similarity
Nucleotide binding279 – 29113NAD By similarity

Sites

Metal binding2221Magnesium HAMAP MF_01033
Metal binding2461Magnesium HAMAP MF_01033
Binding site951Substrate HAMAP MF_01033
Binding site1051Substrate HAMAP MF_01033
Binding site1331Substrate HAMAP MF_01033
Binding site2221Substrate HAMAP MF_01033
Site1401Important for catalysis By similarity
Site1901Important for catalysis By similarity

Secondary structure

1 ...................................................................... 358
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q56268-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 139AFDC3E2CD2060

FASTA35838,462
        10         20         30         40         50         60 
MKKIAIFAGD GIGPEIVAAA RQVLDAVDQA AHLGLRCTEG LVGGAALDAS DDPLPAASLQ 

        70         80         90        100        110        120 
LAMAADAVIL GAVGGPRWDA YPPAKRPEQG LLRLRKGLDL YANLRPAQIF PQLLDASPLR 

       130        140        150        160        170        180 
PELVRDVDIL VVRELTGDIY FGQPRGLEVI DGKRRGFNTM VYDEDEIRRI AHVAFRAAQG 

       190        200        210        220        230        240 
RRKQLCSVDK ANVLETTRLW REVVTEVARD YPDVRLSHMY VDNAAMQLIR APAQFDVLLT 

       250        260        270        280        290        300 
GNMFGDILSD EASQLTGSIG MLPSASLGEG RAMYEPIHGS APDIAGQDKA NPLATILSVA 

       310        320        330        340        350 
MMLRHSLNAE PWAQRVEAAV QRVLDQGLRT ADIAAPGTPV IGTKAMGAAV VNALNLKD

« Hide

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References

[1]"3-isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization."
Kawaguchi H., Inagaki K., Kuwata Y., Tanaka H., Tano T.
J. Biochem. 114:370-377(1993) [PubMed: 8282728] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: AP19-3.
[2]"Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0-A resolution: the role of Glu88 in the unique substrate-recognition mechanism."
Imada K., Inagaki K., Matsunami H., Kawaguchi H., Tanaka H., Tanaka N., Namba K.
Structure 6:971-982(1998) [PubMed: 9739088] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS, SUBUNIT.
Strain: AP19-3.

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Cross-references

Sequence databases

D14585 Genomic DNA. Translation: BAA03437.1.
PIRJX0286.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A05X-ray2.00A/B1-358[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.85. 49.

Family and domain databases

HAMAPMF_01033.
[Tree]
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004429. Isopropylmalate_DH.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF13. IPMDH. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. leuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLEU3_THIFE
AccessionPrimary (citable) accession number: Q56268
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents