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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

Catalytic activityi

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster per subunit.UniRule annotation

Pathwayi: L-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leuA)
  2. 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC)
  3. 3-isopropylmalate dehydrogenase (leuB)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi347Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi407Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi410Iron-sulfur (4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • leucine biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:LEUC-MONOMER.
MetaCyc:LEUC-MONOMER.
UniPathwayiUPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydratase large subunitUniRule annotation (EC:4.2.1.33UniRule annotation)
Alternative name(s):
Alpha-IPM isomeraseUniRule annotation
Short name:
IPMIUniRule annotation
Isopropylmalate isomeraseUniRule annotation
Gene namesi
Name:leuCUniRule annotation
Ordered Locus Names:b0072, JW0071
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11576. leuC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved3 Publications
ChainiPRO_00000767452 – 4663-isopropylmalate dehydratase large subunitAdd BLAST465

Proteomic databases

PaxDbiP0A6A6.
PRIDEiP0A6A6.

2D gel databases

SWISS-2DPAGEiP0A6A6.

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
leuDP301264EBI-1113576,EBI-1113528

Protein-protein interaction databases

BioGridi4262050. 14 interactors.
DIPiDIP-35834N.
IntActiP0A6A6. 3 interactors.
STRINGi316407.85674316.

Structurei

3D structure databases

ProteinModelPortaliP0A6A6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CQI. Bacteria.
COG0065. LUCA.
HOGENOMiHOG000226972.
InParanoidiP0A6A6.
KOiK01703.
PhylomeDBiP0A6A6.

Family and domain databases

CDDicd01583. IPMI. 1 hit.
Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1. 1 hit.
InterProiView protein in InterPro
IPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR033941. IPMI_cat.
PfamiView protein in Pfam
PF00330. Aconitase. 1 hit.
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiView protein in PROSITE
PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTLYEKLF DAHVVYEAEN ETPLLYIDRH LVHEVTSPQA FDGLRAHGRP
60 70 80 90 100
VRQPGKTFAT MDHNVSTQTK DINACGEMAR IQMQELIKNC KEFGVELYDL
110 120 130 140 150
NHPYQGIVHV MGPEQGVTLP GMTIVCGDSH TATHGAFGAL AFGIGTSEVE
160 170 180 190 200
HVLATQTLKQ GRAKTMKIEV QGKAAPGITA KDIVLAIIGK TGSAGGTGHV
210 220 230 240 250
VEFCGEAIRD LSMEGRMTLC NMAIEMGAKA GLVAPDETTF NYVKGRLHAP
260 270 280 290 300
KGKDFDDAVA YWKTLQTDEG ATFDTVVTLQ AEEISPQVTW GTNPGQVISV
310 320 330 340 350
NDNIPDPASF ADPVERASAE KALAYMGLKP GIPLTEVAID KVFIGSCTNS
360 370 380 390 400
RIEDLRAAAE IAKGRKVAPG VQALVVPGSG PVKAQAEAEG LDKIFIEAGF
410 420 430 440 450
EWRLPGCSMC LAMNNDRLNP GERCASTSNR NFEGRQGRGG RTHLVSPAMA
460
AAAAVTGHFA DIRNIK
Length:466
Mass (Da):49,882
Last modified:January 23, 2007 - v2
Checksum:i2B225514207C5EFA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74A → G in BAA21004 (PubMed:8119295).Curated1
Sequence conflicti74A → G in BAA21005 (PubMed:8119295).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73183.1.
AP009048 Genomic DNA. Translation: BAB96641.2.
D17631 Genomic DNA. Translation: BAA21004.1.
D17632 Genomic DNA. Translation: BAA21005.1.
PIRiH64728.
RefSeqiNP_414614.1. NC_000913.3.
WP_001140652.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73183; AAC73183; b0072.
BAB96641; BAB96641; BAB96641.
GeneIDi945076.
KEGGiecj:JW0071.
eco:b0072.
PATRICifig|1411691.4.peg.2209.

Similar proteinsi

Entry informationi

Entry nameiLEUC_ECOLI
AccessioniPrimary (citable) accession number: P0A6A6
Secondary accession number(s): P30127, P78042, Q8FL77
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 102 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families