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Reviewed, UniProtKB/Swiss-Prot Q7NUC2 (LEU3_CHRVO)

Last modified November 4, 2008. Version 44. 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
Ordered Locus Names: CV_2778
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length354 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.

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + 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

CytoplasmBy 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 – 3543543-isopropylmalate dehydrogenase
PRO_0000083679

Regions

Nucleotide binding73 – 8614NAD By similarity
Nucleotide binding279 – 29113NAD By similarity

Sites

Metal binding2211Magnesium or manganese By similarity
Metal binding2451Magnesium or manganese By similarity
Metal binding2491Magnesium or manganese By similarity
Binding site931Substrate By similarity
Binding site1031Substrate By similarity
Binding site1311Substrate By similarity
Binding site2211Substrate By similarity
Site1381Important for catalysis By similarity
Site1891Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NUC2-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 3DA41DB62D0E15B6

FASTA35438,544
        10         20         30         40         50         60 
MKIAILPGDG IGPEIIAQAE RVLEVLRRDG LKIETEHAPL GGAAYDQYGV PYPEATQKLA 

        70         80         90        100        110        120 
READAVLLGA VGGPAYDKLD RPLRPERGLL AIRKDLNLFA NLRPAILYPE LANASTLKPE 

       130        140        150        160        170        180 
VVAGLDIMIV RELTGDIYFG QPRGIAVNEL GEREAYNTMR YSESEVRRIA HVAFGIAMKR 

       190        200        210        220        230        240 
NRKLCSVDKA NVLETTEFWK EIMIEVAKEY PQVELSHMYV DNAAMQLVRN PKQFDVMVTG 

       250        260        270        280        290        300 
NIFGDILSDE ASMLTGSIGM LPSASLDQNN KGLYEPSHGS APDIAGQNLA NPLATILSAA 

       310        320        330        340        350 
MMLRYSFGQE AAARRVEDAV KKVLAQGYRT ADIYEAGCEK VSCSGMGDAV VAAM 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ60446.1.
RefSeqNP_902448.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2547144.
GenomeReviewsGene locus CV_2778 in contig AE016825_GR.
KEGGcvi:CV_2778.
NMPDRfig|243365.1.peg.2778.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7NUC2.

Enzyme and pathway databases

BioCycCVIO243365:CV_2778-MON.

Family and domain databases

HAMAPMF_01033.
[Tree]
InterProIPR004429. 3-isopropylmalate_DHase.
IPR001804. IsoCit_IM_DHase.
[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_CHRVO
AccessionPrimary (citable) accession number: Q7NUC2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: November 4, 2008
This is version 44 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