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Q5E858 (LEUC_VIBF1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:VF_0293
OrganismVibrio fischeri (strain ATCC 700601 / ES114) [Reference proteome] [HAMAP]
Taxonomic identifier312309 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length471 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 – 4714713-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
PRO_0000076837

Sites

Metal binding3491Iron-sulfur (4Fe-4S) By similarity
Metal binding4091Iron-sulfur (4Fe-4S) By similarity
Metal binding4121Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E858 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: CA514DE363251123

FASTA47150,470
        10         20         30         40         50         60 
MSNAKTLYEK IYDAHVAVAA EGENPILYID RHLVHEVTSP QAFDGLREKG RKVRQVGKTF 

        70         80         90        100        110        120 
ATMDHNVSTQ TKDINASGEM ARIQMETLSK NCEEFGVTLY DLNHKYQGIV HVMGPELGIT 

       130        140        150        160        170        180 
LPGMTIVCGD SHTATHGAFG SLAFGIGTSE VEHVLATQTL KQARAKTMKI DVKGKVAEGI 

       190        200        210        220        230        240 
TAKDIVLAII GKTTAAGGTG YVVEFCGEAI TDLTMEGRMT VCNMAIELGA KAGLIAPDQT 

       250        260        270        280        290        300 
TFDYIAGRKF SPQDADLDAA IEYWSSLKTD DDAEFDAVVT LDASEIKPQV TWGTNPGQVI 

       310        320        330        340        350        360 
AVDAPIPAPE SFADPVEKAS AEKALAYMGL EAGKSLSDYN VDKVFVGSCT NSRIEDMRAA 

       370        380        390        400        410        420 
AAIAKGRKVA SHVQALIVPG SEQVKAQAEK EGLDVIFKEA GFEWRLPGCS MCLAMNNDRL 

       430        440        450        460        470 
GPHERCASTS NRNFEGRQGR DGRTHLVSPA MAAAAAIAGH FVDIRTITEQ A 

« Hide

References

[1]"Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with pathogenic congeners."
Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R., Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E., Stevens A., Visick K., Whistler C., Greenberg E.P.
Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700601 / ES114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000020 Genomic DNA. Translation: AAW84788.1.
RefSeqYP_203676.1. NC_006840.2.

3D structure databases

ProteinModelPortalQ5E858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312309.VF_0293.

Protocols and materials databases

DNASU3277251.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW84788; AAW84788; VF_0293.
GeneID3277251.
KEGGvfi:VF_0293.
PATRIC20111060. VBIVibFis127983_0287.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAFIS312309:GIWP-289-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.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_VIBF1
AccessionPrimary (citable) accession number: Q5E858
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 65 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