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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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

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

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
MINTiP80858
STRINGi224308.Bsubs1_010100015436

Structurei

3D structure databases

ProteinModelPortaliP80858
SMRiP80858
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
OMAiFDHQVPA
PhylomeDBiP80858

Family and domain databases

CDDicd01583 IPMI, 1 hit
Gene3Di3.30.499.10, 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
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
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

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
PATRICifig|224308.179.peg.3070

Similar proteinsi

Entry informationi

Entry nameiLEUC_BACSU
AccessioniPrimary (citable) accession number: P80858
Secondary accession number(s): P94567
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 129 of the entry and version 1 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

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