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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

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. no protein annotated in this organism
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 bindingi350Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi410Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi413Iron-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

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:BMEI0157
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000767131 – 4693-isopropylmalate dehydratase large subunitAdd BLAST469

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Protein-protein interaction databases

STRINGi224914.BAWG_0039

Structurei

3D structure databases

ProteinModelPortaliQ8YJC9
SMRiQ8YJC9
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
KOiK01703
OMAiFDHQVPA

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
PS01244 ACONITASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q8YJC9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAPRTLYDK IWDDHVVDQQ EDGTCLLYID RHLVHEVTSP QAFEGLHMAG
60 70 80 90 100
RPVRHPEKTL AVVDHNVPTS PDRINGIQNE ESRIQVEALA RNAADFGVEY
110 120 130 140 150
YSERDKRQGI VHIVGPEQGF TLPGMTIVCG DSHTSTHGAF GALAHGIGTS
160 170 180 190 200
EVEHVLATQT LIQKKAKNML VRVDGKLPAG VTAKDIVLAI IGEIGTAGGT
210 220 230 240 250
GYVIEYAGEA IRSLSMEGRM TICNMSIEGG ARAGLIAPDE TTFEYIKGRP
260 270 280 290 300
RAPQGETLEQ AINYWKTLHS DEGAHFDKIV TLDAGSLPPI VSWGSSPEDV
310 320 330 340 350
VSVTGVVPNP DDIADETKRA SKWRALDYMG LKPGTKITDI AVDRVFIGSC
360 370 380 390 400
TNGRIEDLRA AAKVVEGKKV APTVNAMIVP GSGLVKEQAE AEGLHKIFIE
410 420 430 440 450
AGFDWREPGC SMCLAMNDDR LKPGERCAST SNRNFEGRQG FKGRTHLVSP
460
AMAAAAAIAG HFVDIRAWK
Length:469
Mass (Da):50,692
Last modified:March 1, 2002 - v1
Checksum:i14442D949C40BCDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA Translation: AAL51339.1
PIRiAH3271
RefSeqiWP_004684442.1, NZ_GG703778.1

Genome annotation databases

EnsemblBacteriaiAAL51339; AAL51339; BMEI0157
GeneIDi29594568
KEGGibme:BMEI0157
bmel:DK63_1278
PATRICifig|224914.52.peg.1347

Similar proteinsi

Entry informationi

Entry nameiLEUC_BRUME
AccessioniPrimary (citable) accession number: Q8YJC9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 1, 2002
Last modified: March 28, 2018
This is version 105 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
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Main funding by: National Institutes of Health