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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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 large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD)
  3. 3-isopropylmalate dehydrogenase (leuB)
  4. Probable 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)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:SCO5553
ORF Names:SC1C2.34
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000768261 – 4763-isopropylmalate dehydratase large subunitAdd BLAST476

Proteomic databases

PRIDEiO86534

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO5553

Structurei

3D structure databases

ProteinModelPortaliO86534
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
InParanoidiO86534
KOiK01703
OMAiFDHQVPA
OrthoDBiPOG091H02GD
PhylomeDBiO86534

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.

O86534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRTLAEKVW DDHVVRRAEG EPDLLFIDLH LLHEVTSPQA FDGLRKSGRP
60 70 80 90 100
VRRLDLTIAT EDHNTPTLDI DKPIADPVSR AQLETLRKNC ADFGVRLHPL
110 120 130 140 150
GDVEQGVVHV VGPQLGLTQP GTTVVCGDSH TSTHGAFGAL AFGIGTSQVE
160 170 180 190 200
HVLATQTLPL ARPKTMAITV DGELPEGVTA KDLILAIIAR IGTGGGQGYI
210 220 230 240 250
LEYRGEAIEK LSMEARMTIC NMSIEAGARA GMIAPDETTF AYLQGRPHAP
260 270 280 290 300
EGADWDAAVE YWKTLRTDDD AEFDAEVVIE AAELAPFVTW GTNPGQGAPL
310 320 330 340 350
SAAVPDPASY EDASERFAAE KALEYMGLEA GQPLRSIQVD TVFVGSCTNG
360 370 380 390 400
RIEDLRAAAE IVRDRKVADG VRMLVVPGSA RVGLQAVSEG LDVVFKEAGA
410 420 430 440 450
EWRHAGCSMC LGMNPDQLAP GERSASTSNR NFEGRQGKGG RTHLVSPQVA
460 470
AATAVLGHLA SPADLSAADV PTPAGV
Length:476
Mass (Da):50,480
Last modified:November 1, 1998 - v1
Checksum:i89C3921EFB125109
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939124 Genomic DNA Translation: CAA20001.1
PIRiT29083
RefSeqiNP_629687.1, NC_003888.3
WP_003973442.1, NC_003888.3

Genome annotation databases

EnsemblBacteriaiCAA20001; CAA20001; CAA20001
GeneIDi1100993
29662732
KEGGisco:SCO5553
PATRICifig|100226.15.peg.5641

Similar proteinsi

Entry informationi

Entry nameiLEUC_STRCO
AccessioniPrimary (citable) accession number: O86534
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: November 1, 1998
Last modified: March 28, 2018
This is version 113 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, Reference proteome
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Main funding by: National Institutes of Health