Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
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 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

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:BUsg_PL6
Encoded oniPlasmid pLeu-Sg (pBSg1)0 Publication
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera
Proteomesi
  • UP000000416 Componenti: Plasmid pLeu-Sg

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000767211 – 4693-isopropylmalate dehydratase large subunitAdd BLAST469

Proteomic databases

PRIDEiO85065

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO85065
SMRiO85065
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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.

O85065-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTLYEKIY DAHIVHEEKN NISILYIDLH LLHEVTSPQA FDSLRMRNRS
60 70 80 90 100
VRQPKKTFAT MDHNVSTESK DINASGSMAK IQMQQLIKNC EEFNIALYDL
110 120 130 140 150
NNPKQGIVHV IGPEQGLTLP GSTIVCGDSH TSTHGAFGAL SFGIGTSEVE
160 170 180 190 200
HVLVTQTLKQ QRFKNMKIKI VGKVKKFITA KDIILFIIGK LGTSSGSGYV
210 220 230 240 250
IEFCGDVIKK MNMEERMTIC NMAIEMGAKS ALIAPDETTY LYLKNKRYSP
260 270 280 290 300
KNKYWDSAIR YWKTLVTDEN ALFDKEFTFD ISDISPQVTW GTSPDQVLSI
310 320 330 340 350
NEKIPDFNSF KDSIKKDLAR SACNYMDLKP GSYLKNIKID KVFIGSCTNS
360 370 380 390 400
RIEDLRSAAT ILKNKKISKN IKAIVVPGSG SVKNQAEKEG LDKIFIDAGF
410 420 430 440 450
EWRLPGCSMC LGMNNDKLSD GERCASTSNR NFEGRQGRGG RTHLVSPIMA
460
AAAIYGHFVD VRNLNSETN
Length:469
Mass (Da):52,426
Last modified:November 1, 1998 - v1
Checksum:i4094EC232646228B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041836 Genomic DNA Translation: AAD12595.1
RefSeqiNP_047182.1, NC_001910.1

Genome annotation databases

GeneIDi2648306

Similar proteinsi

Entry informationi

Entry nameiLEUC_BUCAP
AccessioniPrimary (citable) accession number: O85065
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: November 1, 1998
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, Plasmid

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health