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Q7NUB8 (LEUD2_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. Feed History...

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

EC=4.2.1.33
Alternative name(s):
Alpha-IPM isomerase 2
Short name=IPMI 2
Isopropylmalate isomerase 2
Gene names
Name:leuD2
Ordered Locus Names:CV_2782
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01031

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01031

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01031

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01031

Sequence similarities

Belongs to the LeuD family. LeuD type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Branched-chain amino acid biosynthesis
Leucine biosynthesis
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processleucine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_component3-isopropylmalate dehydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function3-isopropylmalate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2122123-isopropylmalate dehydratase small subunit 2 HAMAP-Rule MF_01031
PRO_0000141811

Sequences

Sequence LengthMass (Da)Tools
Q7NUB8 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: FD5CB8726E1980C2

FASTA21223,768
        10         20         30         40         50         60 
MKAFTTLQGL VCPLDRANVD TDAIIPKQFL KSIKRSGFGP NLFDEWRYLD HGEPGMDNAK 

        70         80         90        100        110        120 
RPLNPDFVLN QPRYQGAQVL LARENFGCGS SREHAPWALD DQGFRVVIAP SFADIFFNNC 

       130        140        150        160        170        180 
YKNGLLPIVL AADIVDQLFQ ECEAAPGYSL KVDLAAQTVF TPSGQAFLFD ITEHRKHCLL 

       190        200        210 
GGLDEIGLTL QHADEIKAFE ARRRVEQPWL FA 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ60450.1.
RefSeqNP_902452.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NUB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_2782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ60450; AAQ60450; CV_2782.
GeneID2548220.
KEGGcvi:CV_2782.
PATRIC21440306. VBIChrVio67196_2705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0066.
HOGENOMHOG000222939.
KOK01704.
OMAAFTTHTG.
OrthoDBEOG661HCP.
ProtClustDBPRK01641.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-2841-MONOMER.
UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
HAMAPMF_01031. LeuD_type1.
InterProIPR004431. 3-IsopropMal_deHydase_ssu.
IPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMSSF52016. SSF52016. 1 hit.
TIGRFAMsTIGR00171. leuD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLEUD2_CHRVO
AccessionPrimary (citable) accession number: Q7NUB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 77 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

PATHWAY comments

Index of metabolic and biosynthesis pathways