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Reviewed, UniProtKB/Swiss-Prot Q9EVG9 (LEU3_BUCUM)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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
Encoded onPlasmid pLeu (pBAp1)
OrganismBuchnera aphidicola subsp. Uroleucon ambrosiae
Taxonomic identifier118117 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. HAMAP MF_01033

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3653653-isopropylmalate dehydrogenase HAMAP MF_01033
PRO_0000083664

Regions

Nucleotide binding78 – 9114NAD By similarity
Nucleotide binding287 – 29913NAD By similarity

Sites

Metal binding2291Magnesium or manganese By similarity
Metal binding2531Magnesium or manganese By similarity
Metal binding2571Magnesium or manganese By similarity
Binding site991Substrate By similarity
Binding site1091Substrate By similarity
Binding site1391Substrate By similarity
Binding site2291Substrate By similarity
Site1461Important for catalysis By similarity
Site1971Important for catalysis By similarity

Natural variations

Natural variant2551V → I in strain: GA2181.

Sequences

Sequence LengthMass (Da)Tools
Q9EVG9-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 14F1E76B771C5764

FASTA36540,759
        10         20         30         40         50         60 
MKTKYRISVL PGDGIGPEVM REAYKILNIL KNHFSLPLEI KEFNIGGAAI DQEGVALPKK 

        70         80         90        100        110        120 
TLLGCENSDA ILFGSVGGKK WDHLPIDKRP ERASLLPLRK HFNLFANLRP AQLYSELKYL 

       130        140        150        160        170        180 
SPLRSDIXIK NGFNILCIRE LTGGIYFGKP TGRXLKKNNI EYAFDTEIYY DYEINRIAHL 

       190        200        210        220        230        240 
AFQLAQTRNY KVCSIDKSNV LNSSVLWRET VQKVSKNYPD VHLSHLYIDN ATMQIIKDPN 

       250        260        270        280        290        300 
QFDILLCSNL FGDIVSDECA IITGSIGMLP SASLNEKKFG LYEPAGGSAP DIEGKNIANP 

       310        320        330        340        350        360 
IAQILSVSML VRYGMNLKKI ADKIDQSVIS VLKKGYRTAD ISNNNNYLKT NEMGDVIANT 


LISGE 

« Hide

References

[1]"Vertical transmission of biosynthetic plasmids in aphid endosymbionts (Buchnera)."
Wernegreen J.J., Moran N.A.
J. Bacteriol. 183:785-790(2001) [PubMed: 11133977] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Intraspecific variation in symbiont genomes: bottlenecks and the aphid-Buchnera association."
Funk D.J., Wernegreen J.J., Moran N.A.
Genetics 157:477-489(2001) [PubMed: 11156972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 245-365.
Strain: AL.012, AZ.023, AZ.026, AZ.065, AZ.180, DC.005, GA.039, GA2181, IL.014, IL2.17, IN.018, KY.172, KY2.37, LA.013, MI.035, MN.001, MNb027, MS.040, NY.016, OH.036, TN.173, TN2.38, UT.002 and VA.015.

Cross-references

Sequence databases

AF197454 Genomic DNA. Translation: AAG31396.1.
AF196403 Genomic DNA. Translation: AAK21724.1.
AF196404 Genomic DNA. Translation: AAK21725.1.
AF196407 Genomic DNA. Translation: AAK21730.1.
AF196408 Genomic DNA. Translation: AAK21732.1.
AF196410 Genomic DNA. Translation: AAK21736.1.
AF196412 Genomic DNA. Translation: AAK21740.1.
AF196413 Genomic DNA. Translation: AAK21742.1.
AF196414 Genomic DNA. Translation: AAK21744.1.
AF196415 Genomic DNA. Translation: AAK21746.1.
AF196417 Genomic DNA. Translation: AAK21750.1.
AF196418 Genomic DNA. Translation: AAK21752.1.
AF196419 Genomic DNA. Translation: AAK21754.1.
AF196420 Genomic DNA. Translation: AAK21756.1.
AF196421 Genomic DNA. Translation: AAK21758.1.
AF196422 Genomic DNA. Translation: AAK21760.1.
AF196423 Genomic DNA. Translation: AAK21762.1.
AF196424 Genomic DNA. Translation: AAK21764.1.
AF196402 Genomic DNA. Translation: AAK21722.1.
AF196406 Genomic DNA. Translation: AAK21728.1.
AF196416 Genomic DNA. Translation: AAK21748.1.
AF196425 Genomic DNA. Translation: AAK21766.1.
AF196409 Genomic DNA. Translation: AAK21734.1.
AF196411 Genomic DNA. Translation: AAK21738.1.
AF196405 Genomic DNA. Translation: AAK21727.1.

3D structure databases

HSSPHSSP built from PDB template 1CNZ based on UniProtKB P37412.
ModBaseSearch...

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...

Entry information

Entry nameLEU3_BUCUM
AccessionPrimary (citable) accession number: Q9EVG9
Secondary accession number(s): Q99Q96 expand/collapse secondary AC list , Q99QE7, Q9AJ51, Q9AJ53, Q9AJ54
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 48 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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