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B4F196 (LEUC_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PMI2086
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

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-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 – 4694693-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
PRO_1000135704

Sites

Metal binding3471Iron-sulfur (4Fe-4S) By similarity
Metal binding4071Iron-sulfur (4Fe-4S) By similarity
Metal binding4101Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4F196 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: DE38599BC6906AC6

FASTA46950,440
        10         20         30         40         50         60 
MGKTLYQKIY DAHVVREVAN ETPIIYIDRH LVHEVTSPQA FDGLRTKGRA VRQPNKTFAT 

        70         80         90        100        110        120 
MDHNVSTQTK DINACGDMAR IQMQELMKNC QEFGVTLYDL NHPYQGIVHV MGPEQGLTLP 

       130        140        150        160        170        180 
GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ SRAKTLKIEV QGKTANGITA 

       190        200        210        220        230        240 
KDIVLAIIGK LGSAGGTGYI IEFTGEAIEA LSMEGRMTLC NMAIEMGAKA GLVAPDETTF 

       250        260        270        280        290        300 
AYLKGRQFAP QAPLWDEAVA YWKTLKSDED AIFDATVTIN AAEIAPQVTW GTNPGQVIAI 

       310        320        330        340        350        360 
DQIVPRLNSF NDPVERASAE KALAYMGLTE GVNLTDITID KVFIGSCTNS RIEDLRAAAK 

       370        380        390        400        410        420 
IAKGHKVASH VQAIVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP 

       430        440        450        460 
GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAIHGHFA DIRTFATVS 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR44169.1.
RefSeqYP_002151805.1. NC_010554.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI2086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR44169; CAR44169; PMI2086.
GeneID6800024.
KEGGpmr:PMI2086.
PATRIC20518851. VBIProMir120933_2035.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01703.
OMAQARAKTM.
OrthoDBEOG600DP5.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-2122-MONOMER.
UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 3 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.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_PROMH
AccessionPrimary (citable) accession number: B4F196
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 42 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