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A2C088 (LEUC_PROM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:NATL1_03341
OrganismProchlorococcus marinus (strain NATL1A) [Complete proteome] [HAMAP]
Taxonomic identifier167555 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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_1000063583

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
A2C088 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 5289B9679BD1EB9E

FASTA46951,032
        10         20         30         40         50         60 
MSSRTLYDKV WNFHQVKELP GGSTQLFIGL HLIHEVTSPQ AFSALNEKKL GVKFPNLTVA 

        70         80         90        100        110        120 
TVDHIVPTSN QQRPFSDPLA EEMLSTLEKN CKTHGIKFHG IGSNSQGVVH VMAPELGLTQ 

       130        140        150        160        170        180 
PGMTVACGDS HTSTHGAFGA IAFGIGTSQV RDVLASQSLA MNKLKVRRIW VEGELQKGVY 

       190        200        210        220        230        240 
AKDLILHIIR HLGVKGGVGF AYEFAGPAIE KLSMEGRMTI CNMAIEGGAR CGYINPDETT 

       250        260        270        280        290        300 
FKYLKGKEHA PKGQEWDKAI SWWKSLASDS KATFDDEIQL DGSSIEPTVT WGITPGQGIS 

       310        320        330        340        350        360 
IKETIPNPEF LPKNEQQIAK DACKYMNLKP DEPIEGQSID VCFIGSCTNG RLSDLQEASK 

       370        380        390        400        410        420 
IVKGNTVADG IRAFVVPGSQ KVAKEAKEKG LDKIFLKAGF EWREPGCSMC LAMNPDKLEG 

       430        440        450        460 
RQISASSSNR NFKGRQGSAK GRTLLMSPAM VAAAAINGRV TDVRKFLQE 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL1A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000553 Genomic DNA. Translation: ABM74898.1.
RefSeqYP_001014163.1. NC_008819.1.

3D structure databases

ProteinModelPortalA2C088.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167555.NATL1_03341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM74898; ABM74898; NATL1_03341.
GeneID4779767.
KEGGpme:NATL1_03341.
PATRIC23018193. VBIProMar31285_0341.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01703.
OMAQARAKTM.
OrthoDBEOG600DP5.

Enzyme and pathway databases

BioCycPMAR167555:GI3K-339-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_PROM1
AccessionPrimary (citable) accession number: A2C088
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 20, 2007
Last modified: May 14, 2014
This is version 55 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