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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Buchnera aphidicola subsp. Thelaxes suberi
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi347 – 3471Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi407 – 4071Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi410 – 4101Iron-sulfur (4Fe-4S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Keywords - Ligandi

4Fe-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
Encoded oniPlasmid pBTs10 Publication
OrganismiBuchnera aphidicola subsp. Thelaxes suberi
Taxonomic identifieri98797 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4664663-isopropylmalate dehydratase large subunitPRO_0000076722Add
BLAST

Proteomic databases

PRIDEiO31293.

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO31293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1.
InterProiIPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 2 hits.
PfamiPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQTLYEKLY NSHIIYEDKN TLPIIYIDLH LLHEVTSPQA FESLKNKKRI
60 70 80 90 100
VHAPIKTFAT MDHNVSTKTN KISASGKAAQ IQMQQLINNC KDFNIKLYDL
110 120 130 140 150
NHINQGIVHV MGPEQGLTLP GMTIVCGDSH TSTHGAFGTL AFGIGTSEVE
160 170 180 190 200
HVLATQTLKQ ARSKTMKIGI NGILKPYITA KDVILYIIKK VGTAFGTGYV
210 220 230 240 250
VEFSGETIEN LTMEGRMTIC NMVIEMGAKS GIIAPDATTY KYLKNLPYAP
260 270 280 290 300
KKEKWKNALE YWKNLKTDND AKFDKIVKFD VSQIEPQITW GTNPSQTINI
310 320 330 340 350
TESNPDPKKI NNIIDKQATE KALKYMNLKP NQKMINLVVD KVFIGSCTNS
360 370 380 390 400
RIEDLRIASK IIKNKKVAKT TKAIVVPGSK LVKIQAEKEG LDKIFINAGF
410 420 430 440 450
EWRLPGCSMC LAMNDDKLNR GERCASTSNR NFEDRQGRGG RTHLVSPITA
460
AAAAIFGYFV DIKNIL
Length:466
Mass (Da):51,930
Last modified:January 1, 1998 - v1
Checksum:iA63877597C846ADB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11966 Genomic DNA. Translation: CAA72703.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11966 Genomic DNA. Translation: CAA72703.1.

3D structure databases

ProteinModelPortaliO31293.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO31293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00048; UER00071.

Family and domain databases

Gene3Di3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPiMF_01026. LeuC_type1.
InterProiIPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 2 hits.
PfamiPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00170. leuC. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Putative evolutionary origin of plasmids carrying the genes involved in leucine biosynthesis in Buchnera aphidicola (endosymbiont of aphids)."
    van Ham R.C.H.J., Moya A., Latorre A.
    J. Bacteriol. 179:4768-4777(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiLEUC_BUCTS
AccessioniPrimary (citable) accession number: O31293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.