Skip Header

Contribute Send feedback
Read comments (?) or add your own

C0RFF1 (LEUC_BRUMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. 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
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 large subunit
EC=4.2.1.33
Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase
Gene names
Name:leuC
Ordered Locus Names:BMEA_A1961
OrganismBrucella melitensis biotype 2 (strain ATCC 23457) [Complete proteome] [HAMAP]
Taxonomic identifier546272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length469 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 MF_01026

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01026

(2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP MF_01026

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP MF_01026

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP MF_01026

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP MF_01026

Sequence similarities

Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4694693-isopropylmalate dehydratase large subunit HAMAP MF_01026
PRO_1000149356

Sites

Metal binding3501Iron-sulfur (4Fe-4S) By similarity
Metal binding4101Iron-sulfur (4Fe-4S) By similarity
Metal binding4131Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
C0RFF1 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 14442D949C40BCDF

FASTA46950,692
        10         20         30         40         50         60 
MSAPRTLYDK IWDDHVVDQQ EDGTCLLYID RHLVHEVTSP QAFEGLHMAG RPVRHPEKTL 

        70         80         90        100        110        120 
AVVDHNVPTS PDRINGIQNE ESRIQVEALA RNAADFGVEY YSERDKRQGI VHIVGPEQGF 

       130        140        150        160        170        180 
TLPGMTIVCG DSHTSTHGAF GALAHGIGTS EVEHVLATQT LIQKKAKNML VRVDGKLPAG 

       190        200        210        220        230        240 
VTAKDIVLAI IGEIGTAGGT GYVIEYAGEA IRSLSMEGRM TICNMSIEGG ARAGLIAPDE 

       250        260        270        280        290        300 
TTFEYIKGRP RAPQGETLEQ AINYWKTLHS DEGAHFDKIV TLDAGSLPPI VSWGSSPEDV 

       310        320        330        340        350        360 
VSVTGVVPNP DDIADETKRA SKWRALDYMG LKPGTKITDI AVDRVFIGSC TNGRIEDLRA 

       370        380        390        400        410        420 
AAKVVEGKKV APTVNAMIVP GSGLVKEQAE AEGLHKIFIE AGFDWREPGC SMCLAMNDDR 

       430        440        450        460 
LKPGERCAST SNRNFEGRQG FKGRTHLVSP AMAAAAAIAG HFVDIRAWK

« Hide

References

[1]"Brucella melitensis ATCC 23457 whole genome shotgun sequencing project."
Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C. expand/collapse author list , Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23457.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001488 Genomic DNA. Translation: ACO01623.1.
RefSeqYP_002733577.1. NC_012441.1.

3D structure databases

ProteinModelPortalC0RFF1.
ModBaseSearch...

Protein-protein interaction databases

STRINGC0RFF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7677608.
GenomeReviewsGene locus BMEA_A1961 in contig CP001488_GR.
KEGGbmi:BMEA_A1961.
PATRIC17839718. VBIBruMel14466_1976.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMADIRQGIV.
ProtClustDBPRK05478.

Family and domain databases

HAMAPMF_01026. LeuC_type1.
[Tree]
InterProIPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR015936. Homoacnase/3IPM_deHydtase_su.
[Graphical view]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 3 hits.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KOK01703.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF6. Homoacnase/3IPM_dehydase_s/lsu. 1 hit.
PfamPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR00170. LeuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_BRUMB
AccessionPrimary (citable) accession number: C0RFF1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: January 25, 2012
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents