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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi347 – 3471Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi407 – 4071Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi410 – 4101Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

  • 3-isopropylmalate dehydratase activity Source: UniProtKB-HAMAP
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • hydro-lyase activity Source: EcoCyc
  • intramolecular transferase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • leucine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:LEUC-MONOMER.
ECOL316407:JW0071-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11576. leuC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 4664653-isopropylmalate dehydratase large subunitPRO_0000076745Add
BLAST

Proteomic databases

EPDiP0A6A6.
PaxDbiP0A6A6.
PRIDEiP0A6A6.

2D gel databases

SWISS-2DPAGEP0A6A6.

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 interactions.
DIPiDIP-35834N.
IntActiP0A6A6. 3 interactions.
STRINGi511145.b0072.

Structurei

3D structure databases

ProteinModelPortaliP0A6A6.
SMRiP0A6A6. Positions 4-461.
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.
OMAiCNMSIEM.
OrthoDBiEOG600DP5.
PhylomeDBiP0A6A6.

Family and domain databases

Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1.
InterProiIPR004430. 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]
PANTHERiPTHR11670. PTHR11670. 2 hits.
PfamiPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741A → G in BAA21004 (PubMed:8119295).Curated
Sequence conflicti74 – 741A → G in BAA21005 (PubMed:8119295).Curated

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.
PATRICi32115247. VBIEscCol129921_0075.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP0A6A6.
SMRiP0A6A6. Positions 4-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262050. 14 interactions.
DIPiDIP-35834N.
IntActiP0A6A6. 3 interactions.
STRINGi511145.b0072.

2D gel databases

SWISS-2DPAGEP0A6A6.

Proteomic databases

EPDiP0A6A6.
PaxDbiP0A6A6.
PRIDEiP0A6A6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73183; AAC73183; b0072.
BAB96641; BAB96641; BAB96641.
GeneIDi945076.
KEGGiecj:JW0071.
eco:b0072.
PATRICi32115247. VBIEscCol129921_0075.

Organism-specific databases

EchoBASEiEB1536.
EcoGeneiEG11576. leuC.

Phylogenomic databases

eggNOGiENOG4105CQI. Bacteria.
COG0065. LUCA.
HOGENOMiHOG000226972.
InParanoidiP0A6A6.
KOiK01703.
OMAiCNMSIEM.
OrthoDBiEOG600DP5.
PhylomeDBiP0A6A6.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.
BioCyciEcoCyc:LEUC-MONOMER.
ECOL316407:JW0071-MONOMER.
MetaCyc:LEUC-MONOMER.

Miscellaneous databases

PROiP0A6A6.

Family and domain databases

Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1.
InterProiIPR004430. 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]
PANTHERiPTHR11670. PTHR11670. 2 hits.
PfamiPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Aphidicolin inhibits DNA polymerase II of Escherichia coli, an alpha-like DNA polymerase."
    Rosenthal E.R., Calvo J.M.
    Nucleic Acids Res. 18:7185-7186(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 70 AND 361.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus."
    Kirino H., Aoki M., Aoshima M., Hayashi Y., Ohba M., Yamagishi A., Wakagi T., Oshima T.
    Eur. J. Biochem. 220:275-281(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205.
    Strain: K12.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  7. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. Cited for: PROTEIN SEQUENCE OF 2-5.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiLEUC_ECOLI
AccessioniPrimary (citable) accession number: P0A6A6
Secondary accession number(s): P30127, P78042, Q8FL77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 93 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.