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Protein

3-isopropylmalate dehydratase large subunit

Gene

leuC

Organism
Thermosynechococcus elongatus (strain BP-1)
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

Pathway: 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 (tlr1234), 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 bindingi349 – 3491Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi409 – 4091Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi412 – 4121Iron-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
Ordered Locus Names:tlr0909
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
ProteomesiUP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4694693-isopropylmalate dehydratase large subunitPRO_0000076828Add
BLAST

Interactioni

Subunit structurei

Heterodimer of LeuC and LeuD.UniRule annotation

Protein-protein interaction databases

STRINGi197221.tlr0909.

Structurei

3D structure databases

ProteinModelPortaliQ8DKF0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0065.
HOGENOMiHOG000226972.
KOiK01703.
OMAiDKVWDLH.
OrthoDBiEOG600DP5.

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. 1 hit.
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.

Q8DKF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMSRGTLFD KVWEQHTVAT LPSGQTQLFI GLHLIHEVTS PQAFAMLRER
60 70 80 90 100
GLPVLYPQRT IATVDHIVPT DTLARPLQDA LAEEMLQALE ANCRAHNIPF
110 120 130 140 150
FGIGSGRQGI VHVIAPEQGL TQPGMTIACG DSHTSTHGAF GAIAFGIGTS
160 170 180 190 200
QVRDVLATQT LALNKLKVRK VEVNGSLAAG VYAKDVILHV IRHLGVKGGV
210 220 230 240 250
GYAYEFAGTT FGQLSMEERM TVCNMAIEGG ARCGYVNPDE TTFAYLKGRP
260 270 280 290 300
FAPQGKAWDE AVAWWRSLAS DADAEYDDVV TFAAADIAPT VTWGITPGQS
310 320 330 340 350
VAVDETLPTL ESLPVAERAI AAEAYAYMDL QPGQPIQGTK IDVCFIGSCT
360 370 380 390 400
NGRISDLRQA AKVVEGRKVK PGVKAFVVPG SERVKAQAEA EGLDVVFKAA
410 420 430 440 450
GFEWRNPGCS MCLAMNPDKL QGRQISASSS NRNFKGRQGS PSGRTLLMSP
460
AMVAAAAIAG EVTDVRAFL
Length:469
Mass (Da):50,088
Last modified:March 1, 2003 - v1
Checksum:iD3127080A899B236
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08461.1.
RefSeqiNP_681699.1. NC_004113.1.
WP_011056753.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC08461; BAC08461; BAC08461.
GeneIDi1011413.
KEGGitel:tlr0909.
PATRICi23927110. VBITheElo119873_0955.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC08461.1.
RefSeqiNP_681699.1. NC_004113.1.
WP_011056753.1. NC_004113.1.

3D structure databases

ProteinModelPortaliQ8DKF0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tlr0909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC08461; BAC08461; BAC08461.
GeneIDi1011413.
KEGGitel:tlr0909.
PATRICi23927110. VBITheElo119873_0955.

Phylogenomic databases

eggNOGiCOG0065.
HOGENOMiHOG000226972.
KOiK01703.
OMAiDKVWDLH.
OrthoDBiEOG600DP5.

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. 1 hit.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiLEUC_THEEB
AccessioniPrimary (citable) accession number: Q8DKF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 80 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.