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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Leuconostoc gelidum subsp. gasicomitatum (strain DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

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

Pathway: L-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD)
  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 bindingi339 – 3391Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi399 – 3991Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi402 – 4021Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotation

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

4Fe-4SUniRule annotationSAAS annotation, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciLGAS762550:GHH1-1424-MONOMER.
UniPathwayiUPA00048; UER00071.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydratase large subunitUniRule annotationSAAS annotation (EC:4.2.1.33UniRule annotationSAAS annotation)
Alternative name(s):
Alpha-IPM isomeraseUniRule annotation
Isopropylmalate isomeraseUniRule annotation
Gene namesi
Name:leuCUniRule annotationImported
Ordered Locus Names:LEGAS_0263Imported
OrganismiLeuconostoc gelidum subsp. gasicomitatum (strain DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10)Imported
Taxonomic identifieri762550 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLeuconostocaceaeLeuconostoc
ProteomesiUP000008706 Componenti: Chromosome

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi762550.LEGAS_0263.

Structurei

3D structure databases

ProteinModelPortaliD8MDJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000226972.
KOiK01703.
OMAiDKVWDLH.

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. 1 hit.
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.

D8MDJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTLFDKIW EKHVITGEIG EAQLIYVDLH LIHEVTSPQP FDGLRNTNRR
60 70 80 90 100
VRRPDLTFAT MDHNVSTKDI FNVQDHMSRL QMDTLVKNTK EFGVPLASIG
110 120 130 140 150
DDKQGIVHVV GPERGLTQPA KLIVCGDSHT ATHGAFGAIA FGIGTSEVEH
160 170 180 190 200
VLATQTIWQV KPKTMGIKVT GKLLKNTYAK DIIMGIIAKY GVSFGVGYAI
210 220 230 240 250
EFYGETVENL SMEARMTMCN MSIEAGSRTG MVQPDQTTFD YIEGREQAPK
260 270 280 290 300
DFEAAKNYWL QFYTDDESDF DETLTFDVSN LKPMVTWGTN PGMATPVDQS
310 320 330 340 350
LPAIKDDNDA NANAYEYIGL HPHMKATDIN LDYIFIGSCT NSRYEDLEIA
360 370 380 390 400
ANMMKGHHLA PNVTAWIVPG SRAIRNRAIK SGIAKIFEDA GCEWREPGCS
410 420 430 440 450
ACLAMNPDKI PAGKHVASTS NRNFIGRQGA GSRTHLASPA MVAAAGIAGY
460
FVDITVDEFV
Length:460
Mass (Da):50,606
Last modified:October 5, 2010 - v1
Checksum:i123845047F32D05E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN822744 Genomic DNA. Translation: CBL90911.1.
RefSeqiWP_013231184.1. NC_014319.1.
YP_003771730.1. NC_014319.1.

Genome annotation databases

EnsemblBacteriaiCBL90911; CBL90911; LEGAS_0263.
KEGGilgs:LEGAS_0263.
PATRICi42382166. VBILeuGas160647_0271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN822744 Genomic DNA. Translation: CBL90911.1.
RefSeqiWP_013231184.1. NC_014319.1.
YP_003771730.1. NC_014319.1.

3D structure databases

ProteinModelPortaliD8MDJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi762550.LEGAS_0263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBL90911; CBL90911; LEGAS_0263.
KEGGilgs:LEGAS_0263.
PATRICi42382166. VBILeuGas160647_0271.

Phylogenomic databases

HOGENOMiHOG000226972.
KOiK01703.
OMAiDKVWDLH.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.
BioCyciLGAS762550:GHH1-1424-MONOMER.

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. 1 hit.
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

  1. "Genome sequence and comparative genomics of a food spoilage lactic acid bacterium Leuconostoc gasicomitatum 18811T."
    Johansson P., Paulin L., Vihavainen E.J., Salovuori N., Alatalo E.R., Bjoerkroth J.K., Auvinen P.
    Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10Imported.

Entry informationi

Entry nameiD8MDJ3_LEUGG
AccessioniPrimary (citable) accession number: D8MDJ3
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: June 24, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.