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P07139 (LEU3_CANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydrogenase
Short name=3-IPM-DH
Short name=IMDH
EC=1.1.1.85
Alternative name(s):
Beta-IPM dehydrogenase
Gene names
Name:LEU2
OrganismCandida maltosa (Yeast)
Taxonomic identifier5479 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Catalytic activity

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

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.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3733733-isopropylmalate dehydrogenase
PRO_0000083604

Regions

Nucleotide binding82 – 9312NAD By similarity
Nucleotide binding295 – 30612NAD By similarity

Sites

Metal binding2311Magnesium or manganese By similarity
Metal binding2561Magnesium or manganese By similarity
Metal binding2601Magnesium or manganese By similarity
Binding site1001Substrate By similarity
Binding site1101Substrate By similarity
Binding site1391Substrate By similarity
Binding site2311Substrate By similarity
Site1461Important for catalysis By similarity
Site1981Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P07139 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 256E9886219BA529

FASTA37340,173
        10         20         30         40         50         60 
MSVKTKTITI LPGDHVGTEI VNEAIKVLEA IEAATPYQKI HFDFKHHLIG GAAIDATGVP 

        70         80         90        100        110        120 
LPDDALESAK NSDAVLLGAV GGPKWGTGAL RPEQGLLKIR KELNLYANIR PCNFASDSLL 

       130        140        150        160        170        180 
ELSPLRPEVV KGTNLIIVRE LVGGIYFGDR EEQEESADKQ TAWDTEKYTV DEVTRITRMA 

       190        200        210        220        230        240 
AFMALQHTPP LPIWSLDKAN VLASSRLWRR TVDKVISEEF PTLSVQHQLI DSAAMILIQN 

       250        260        270        280        290        300 
PTKLNGIIIT SNMFGDIISD EASVIPGSLG LLPSASLASL PDTNTAFGLY EPCHGSAPDL 

       310        320        330        340        350        360 
PANKVNPIAT ILSAASMLRL SLDCVKEAEA LEEAVKQVLD KGIRTADLRG TSSTTEVGDA 

       370 
IVEAVTKILK EKA

« Hide

References

[1]"Nucleotide sequencing analysis of a LEU gene of Candida maltosa which complements leuB mutation of Escherichia coli and leu2 mutation of Saccharomyces cerevisiae."
Takagi M., Kobayashi N., Sugimoto M., Fujii T., Watari J., Yano K.
Curr. Genet. 11:451-457(1987) [PubMed: 2897248] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular analysis of a leu2-mutant of Candida maltosa demonstrates the presence of multiple alleles."
Becher D., Schulze S., Kasuske A., Schulze H., Samsonova I.A., Oliver S.G.
Curr. Genet. 26:208-216(1994) [PubMed: 7859302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G587.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X05459 Genomic DNA. Translation: CAA29024.1.
X72940 Genomic DNA. Translation: CAA51445.1.
PIRS48228.

3D structure databases

ProteinModelPortalP07139.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.85. 1125.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
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...

Entry information

Entry nameLEU3_CANMA
AccessionPrimary (citable) accession number: P07139
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 21, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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