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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
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. 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 bindingi408Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi411Iron-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

BioCyciAPLE416269:G1G87-145-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
Gene namesi
Name:leuCUniRule annotation
Ordered Locus Names:APL_0139
OrganismiActinobacillus pleuropneumoniae serotype 5b (strain L20)
Taxonomic identifieri416269 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus
Proteomesi
  • UP000001432 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000635191 – 4693-isopropylmalate dehydratase large subunitAdd BLAST469

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Protein-protein interaction databases

STRINGi416269.APL_0139

Structurei

3D structure databases

SMRiA3MYL1
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
Gene3Di3.30.499.101 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.

A3MYL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTLYEKLF DAHVVYEAAG ETPILYINRH LIHEVTSPQA FDGLRVAGRQ
60 70 80 90 100
VRQIGKTFGT MDHSISTQVR DVNKLEGQAK IQVLELAKNC EANGISLFDM
110 120 130 140 150
QTKEQGIVHV MGPEQGLTLP GMTIVCGDSH TATHGAFGAL AFGIGTSEVE
160 170 180 190 200
HVLATQTLKQ ARAKSMKVEV RGKVNPGITA KDIVLAIIGK TTMAGGTGHV
210 220 230 240 250
VEFCGEAIRN LSMEGRMTVC NMAIEFGAKA GLVAPDETTF AYLKDRPHAP
260 270 280 290 300
KGKDWDDAVE YWTTLKSDDD AVFDSVVVLE AKDIAPQVTW GTNPGQVIGI
310 320 330 340 350
DQVVPNPQEM ADPVTKASAE KALAYIGLDA NTDMKNIPVD QVFIGSCTNS
360 370 380 390 400
RIEDLRAAAA VMKGRKKADN VKRVLVVPGS GLVKEQAEKE GLDKIFIEAG
410 420 430 440 450
AEWRNPGCSM CLGMNDDRLG EWERCASTSN RNFEGRQGRN GRTHLVSPAM
460
AAAAAMFGKF VDIRHVELN
Length:469
Mass (Da):50,705
Last modified:April 3, 2007 - v1
Checksum:iF6DC751553AD0E6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000569 Genomic DNA Translation: ABN73247.1
RefSeqiWP_011848321.1, NC_009053.1

Genome annotation databases

EnsemblBacteriaiABN73247; ABN73247; APL_0139
GeneIDi4848700
KEGGiapl:APL_0139
PATRICifig|416269.6.peg.143

Similar proteinsi

Entry informationi

Entry nameiLEUC_ACTP2
AccessioniPrimary (citable) accession number: A3MYL1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: April 3, 2007
Last modified: March 28, 2018
This is version 77 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