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E1S589 (E1S589_ECOUM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
EC=4.2.1.33 HAMAP-Rule MF_01026
Alternative name(s):
Alpha-IPM isomerase HAMAP-Rule MF_01026
Isopropylmalate isomerase HAMAP-Rule MF_01026
Gene names
Name:leuC HAMAP-Rule MF_01026
Ordered Locus Names:UM146_23155 EMBL ADN73952.1
OrganismEscherichia coli (strain UM146) [Complete proteome] [HAMAP] EMBL ADN73952.1
Taxonomic identifier869729 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length466 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 SAAS SAAS004430

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_01026 SAAS SAAS015931

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01026 SAAS SAAS004430

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01026 SAAS SAAS004430

Sequence similarities

Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. HAMAP-Rule MF_01026

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding3471Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026
Metal binding4071Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026
Metal binding4101Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026

Sequences

Sequence LengthMass (Da)Tools
E1S589 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 2B225514207C5EFA

FASTA46649,882
        10         20         30         40         50         60 
MAKTLYEKLF DAHVVYEAEN ETPLLYIDRH LVHEVTSPQA FDGLRAHGRP VRQPGKTFAT 

        70         80         90        100        110        120 
MDHNVSTQTK DINACGEMAR IQMQELIKNC KEFGVELYDL NHPYQGIVHV MGPEQGVTLP 

       130        140        150        160        170        180 
GMTIVCGDSH TATHGAFGAL AFGIGTSEVE HVLATQTLKQ GRAKTMKIEV QGKAAPGITA 

       190        200        210        220        230        240 
KDIVLAIIGK TGSAGGTGHV VEFCGEAIRD LSMEGRMTLC NMAIEMGAKA GLVAPDETTF 

       250        260        270        280        290        300 
NYVKGRLHAP KGKDFDDAVA YWKTLQTDEG ATFDTVVTLQ AEEISPQVTW GTNPGQVISV 

       310        320        330        340        350        360 
NDNIPDPASF ADPVERASAE KALAYMGLKP GIPLTEVAID KVFIGSCTNS RIEDLRAAAE 

       370        380        390        400        410        420 
IAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF EWRLPGCSMC LAMNNDRLNP 

       430        440        450        460 
GERCASTSNR NFEGRQGRGG RTHLVSPAMA AAAAVTGHFA DIRNIK

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of adherent invasive Escherichia coli UM146 isolated from ileal Crohn's disease biopsy tissue."
Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.
J. Bacteriol. 193:583-583(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UM146 EMBL ADN73952.1.
[2]"Complete genome sequence of adherent invasive Escherichia coli UM146 isolated from ileal Crohn's disease biopsy tissue."
Krause D.O., Little A.C., Dowd S.E., Bernstein C.N.
Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: UM146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002167 Genomic DNA. Translation: ADN73952.1.
RefSeqYP_006113464.1. NC_017632.1.

3D structure databases

ProteinModelPortalE1S589.
SMRE1S589. Positions 4-457.
ModBaseSearch...

Proteomic databases

PRIDEE1S589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADN73952; ADN73952; UM146_23155.
GeneID12703142.
KEGGelu:UM146_23155.
PATRIC42976404. VBIEscCol167775_4981.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226972.
KOK01703.

Enzyme and pathway databases

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. Aconitase_N. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE1S589_ECOUM
AccessionPrimary (citable) accession number: E1S589
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info