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Protein

3-isopropylmalate dehydratase small subunit

Gene

leuD

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.

Pathwayi: L-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
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.

GO - Molecular functioni

  • 3-isopropylmalate dehydratase activity Source: UniProtKB-HAMAP
  • intramolecular transferase activity Source: EcoCyc

GO - Biological processi

  • branched-chain amino acid biosynthetic process Source: UniProtKB-KW
  • 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

Enzyme and pathway databases

BioCyciEcoCyc:LEUD-MONOMER.
ECOL316407:JW0070-MONOMER.
MetaCyc:LEUD-MONOMER.
UniPathwayiUPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydratase small subunit (EC:4.2.1.33)
Alternative name(s):
Alpha-IPM isomerase
Short name:
IPMI
Isopropylmalate isomerase
Gene namesi
Name:leuD
Ordered Locus Names:b0071, JW0070
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11575. leuD.

Subcellular locationi

GO - Cellular componenti

  • 3-isopropylmalate dehydratase complex Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001418192 – 2013-isopropylmalate dehydratase small subunitAdd BLAST200

Proteomic databases

PaxDbiP30126.
PRIDEiP30126.

2D gel databases

SWISS-2DPAGEP30126.

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
leuCP0A6A64EBI-1113528,EBI-1113576

Protein-protein interaction databases

BioGridi4262049. 4 interactors.
DIPiDIP-10092N.
IntActiP30126. 6 interactors.
STRINGi511145.b0071.

Structurei

3D structure databases

ProteinModelPortaliP30126.
SMRiP30126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LeuD family. LeuD type 1 subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105MQS. Bacteria.
COG0066. LUCA.
HOGENOMiHOG000222939.
InParanoidiP30126.
KOiK01704.
OMAiAFTTHTG.
PhylomeDBiP30126.

Family and domain databases

CDDicd01577. IPMI_Swivel. 1 hit.
Gene3Di3.20.19.10. 1 hit.
HAMAPiMF_01031. LeuD_type1. 1 hit.
InterProiIPR004431. 3-IsopropMal_deHydase_ssu.
IPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR033940. IPMI_Swivel.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00171. leuD. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P30126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEKFIKHTG LVVPLDAANV DTDAIIPKQF LQKVTRTGFG AHLFNDWRFL
60 70 80 90 100
DEKGQQPNPD FVLNFPQYQG ASILLARENF GCGSSREHAP WALTDYGFKV
110 120 130 140 150
VIAPSFADIF YGNSFNNQLL PVKLSDAEVD ELFALVKANP GIHFDVDLEA
160 170 180 190 200
QEVKAGEKTY RFTIDAFRRH CMMNGLDSIG LTLQHDDAIA AYEAKQPAFM

N
Length:201
Mass (Da):22,487
Last modified:January 23, 2007 - v3
Checksum:iE5A98B58468E7787
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73182.1.
AP009048 Genomic DNA. Translation: BAB96640.1.
PIRiS40585.
RefSeqiNP_414613.1. NC_000913.3.
WP_000818228.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73182; AAC73182; b0071.
BAB96640; BAB96640; BAB96640.
GeneIDi945642.
KEGGiecj:JW0070.
eco:b0071.
PATRICi32115245. VBIEscCol129921_0074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73182.1.
AP009048 Genomic DNA. Translation: BAB96640.1.
PIRiS40585.
RefSeqiNP_414613.1. NC_000913.3.
WP_000818228.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP30126.
SMRiP30126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262049. 4 interactors.
DIPiDIP-10092N.
IntActiP30126. 6 interactors.
STRINGi511145.b0071.

2D gel databases

SWISS-2DPAGEP30126.

Proteomic databases

PaxDbiP30126.
PRIDEiP30126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73182; AAC73182; b0071.
BAB96640; BAB96640; BAB96640.
GeneIDi945642.
KEGGiecj:JW0070.
eco:b0071.
PATRICi32115245. VBIEscCol129921_0074.

Organism-specific databases

EchoBASEiEB1535.
EcoGeneiEG11575. leuD.

Phylogenomic databases

eggNOGiENOG4105MQS. Bacteria.
COG0066. LUCA.
HOGENOMiHOG000222939.
InParanoidiP30126.
KOiK01704.
OMAiAFTTHTG.
PhylomeDBiP30126.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.
BioCyciEcoCyc:LEUD-MONOMER.
ECOL316407:JW0070-MONOMER.
MetaCyc:LEUD-MONOMER.

Miscellaneous databases

PROiP30126.

Family and domain databases

CDDicd01577. IPMI_Swivel. 1 hit.
Gene3Di3.20.19.10. 1 hit.
HAMAPiMF_01031. LeuD_type1. 1 hit.
InterProiIPR004431. 3-IsopropMal_deHydase_ssu.
IPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR033940. IPMI_Swivel.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00171. leuD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLEUD_ECOLI
AccessioniPrimary (citable) accession number: P30126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 134 of the entry and version 3 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.