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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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 2 (ilvK), Branched-chain-amino-acid transaminase 1 (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

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

BioCyciBSUB:BSU28260-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
Superoxide-inducible protein 10
Short name:
SOI10
Gene namesi
Name:leuCUniRule annotation
Ordered Locus Names:BSU28260
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000767001 – 4723-isopropylmalate dehydratase large subunitAdd BLAST472

Proteomic databases

PaxDbiP80858.
PRIDEiP80858.

Expressioni

Inductioni

By superoxide.

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Protein-protein interaction databases

IntActiP80858. 1 interactor.
MINTiMINT-8365942.
STRINGi224308.Bsubs1_010100015436.

Structurei

3D structure databases

ProteinModelPortaliP80858.
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.
InParanoidiP80858.
KOiK01703.
OMAiIDVCFIG.
PhylomeDBiP80858.

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.
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.
IPR033941. IPMI_cat.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMPRTIIEKI WDQHIVKHGE GKPDLLYIDL HLIHEVTSPQ AFEGLRQKGR
60 70 80 90 100
KVRRPQNTFA TMDHNIPTVN RFEIKDEVAK RQVTALERNC EEFGVRLADL
110 120 130 140 150
HSVDQGIVHV VGPELGLTLP GKTIVCGDSH TSTHGAFGAL AFGIGTSEVE
160 170 180 190 200
HVLSTQTLWQ QRPKTLEVRV DGTLQKGVTA KDVILAVIGK YGVKFGTGYV
210 220 230 240 250
IEYTGEVFRN MTMDERMTVC NMSIEAGARA GLIAPDEVTF EYCKNRKYTP
260 270 280 290 300
KGEEFDKAVE EWKALRTDPG AVYDKSIVLD GNKISPMVTW GINPGMVLPV
310 320 330 340 350
DSEVPAPESF SAEDDKKEAI RAYEYMGLTP HQKIEDIKVE HVFIGSCTNS
360 370 380 390 400
RMTDLRQAAD MIKGKKVADS VRAIVVPGSQ SVKLQAEKEG LDQIFLEAGF
410 420 430 440 450
EWRESGCSMC LSMNNDVVPE GERCASTSNR NFEGRQGKGA RTHLVSPAMA
460 470
AMAAIHGHFV DVRKFYQEKT VV
Length:472
Mass (Da):52,392
Last modified:November 1, 1997 - v1
Checksum:iD48A44E2AE155EF2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11W → L AA sequence (PubMed:9298659).Curated1
Sequence conflicti27Y → T AA sequence (PubMed:9298659).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99533.1.
AL009126 Genomic DNA. Translation: CAB14786.1.
PIRiB69650.
RefSeqiNP_390704.1. NC_000964.3.
WP_003229604.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14786; CAB14786; BSU28260.
GeneIDi937478.
KEGGibsu:BSU28260.
PATRICi18977530. VBIBacSub10457_2954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99533.1.
AL009126 Genomic DNA. Translation: CAB14786.1.
PIRiB69650.
RefSeqiNP_390704.1. NC_000964.3.
WP_003229604.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP80858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP80858. 1 interactor.
MINTiMINT-8365942.
STRINGi224308.Bsubs1_010100015436.

Proteomic databases

PaxDbiP80858.
PRIDEiP80858.

Protocols and materials databases

DNASUi937478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14786; CAB14786; BSU28260.
GeneIDi937478.
KEGGibsu:BSU28260.
PATRICi18977530. VBIBacSub10457_2954.

Phylogenomic databases

eggNOGiENOG4105CQI. Bacteria.
COG0065. LUCA.
HOGENOMiHOG000226972.
InParanoidiP80858.
KOiK01703.
OMAiIDVCFIG.
PhylomeDBiP80858.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.
BioCyciBSUB:BSU28260-MONOMER.

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.
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.
IPR033941. IPMI_cat.
[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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEUC_BACSU
AccessioniPrimary (citable) accession number: P80858
Secondary accession number(s): P94567
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 123 of the entry and version 1 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.