Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5WEN5 (LEUC_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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 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:ABC2640
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length470 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_01026

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01026

Cofactor

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

Pathway

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

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule 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 – 4704703-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
PRO_0000076697

Sites

Metal binding3461Iron-sulfur (4Fe-4S) By similarity
Metal binding4061Iron-sulfur (4Fe-4S) By similarity
Metal binding4091Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WEN5 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 6488DD9B8A8426D1

FASTA47050,857
        10         20         30         40         50         60 
MAKTIIEKIW ESHTVVDESG KPNLLYVDLH MVHEVTSPQA FEGLRLAGRT VRRPDKTFAT 

        70         80         90        100        110        120 
MDHNVPTVNR YDIRDQIART QMETLAANCK QFGIEMVDLD HPENGIVHVI GPELGLTQPG 

       130        140        150        160        170        180 
HVIVCGDSHT STHGAFGAIA FGIGTSEVEH VLATQTIWQS KPKTLEVHIS GRLNEGISAK 

       190        200        210        220        230        240 
DVILAIIAKF GVDIGTGSII EFTGEAIRGM TMEERMTICN MSIEAGAKAG LISPDQVTFD 

       250        260        270        280        290        300 
YLQGRANVPK GEAYDEIVEK WAQLATDPGA TYDRSVTIDA AEIEPMVTWG TNPGQGAGIS 

       310        320        330        340        350        360 
KAVPRLDDAK SEVERRAISQ ALDYMDIKPG TPLSEIEIQH VFIGSCTNSR LSDLRAAAAV 

       370        380        390        400        410        420 
INGRKVAPGV RALIVPGSQR VKKRAEEEGL DQVFKEAGFE WRDSGCSMCL SMNPDVVPEG 

       430        440        450        460        470 
ERCASTSNRN FEGRQGKGAR THLVSPAMAA AAAIAGRFVD VRKMVKAGEC 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD65175.1.
RefSeqYP_176136.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WEN5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC2640.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD65175; BAD65175; ABC2640.
GeneID3204058.
KEGGbcl:ABC2640.
PATRIC18924926. VBIBacCla58185_2815.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01703.
OMADKVWDLH.
OrthoDBEOG600DP5.
ProtClustDBPRK05478.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-2719-MONOMER.
UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPMF_01026. LeuC_type1.
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.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF53732. SSF53732. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_BACSK
AccessionPrimary (citable) accession number: Q5WEN5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 67 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