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Q8DKF0 (LEUC_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydratase large subunit

EC=4.2.1.33
Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase
Gene names
Name:leuC
Ordered Locus Names:tlr0909
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01026

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01026

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_01026

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01026

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01026

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4694693-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
PRO_0000076828

Sites

Metal binding3491Iron-sulfur (4Fe-4S) By similarity
Metal binding4091Iron-sulfur (4Fe-4S) By similarity
Metal binding4121Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DKF0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D3127080A899B236

FASTA46950,088
        10         20         30         40         50         60 
MSMSRGTLFD KVWEQHTVAT LPSGQTQLFI GLHLIHEVTS PQAFAMLRER GLPVLYPQRT 

        70         80         90        100        110        120 
IATVDHIVPT DTLARPLQDA LAEEMLQALE ANCRAHNIPF FGIGSGRQGI VHVIAPEQGL 

       130        140        150        160        170        180 
TQPGMTIACG DSHTSTHGAF GAIAFGIGTS QVRDVLATQT LALNKLKVRK VEVNGSLAAG 

       190        200        210        220        230        240 
VYAKDVILHV IRHLGVKGGV GYAYEFAGTT FGQLSMEERM TVCNMAIEGG ARCGYVNPDE 

       250        260        270        280        290        300 
TTFAYLKGRP FAPQGKAWDE AVAWWRSLAS DADAEYDDVV TFAAADIAPT VTWGITPGQS 

       310        320        330        340        350        360 
VAVDETLPTL ESLPVAERAI AAEAYAYMDL QPGQPIQGTK IDVCFIGSCT NGRISDLRQA 

       370        380        390        400        410        420 
AKVVEGRKVK PGVKAFVVPG SERVKAQAEA EGLDVVFKAA GFEWRNPGCS MCLAMNPDKL 

       430        440        450        460 
QGRQISASSS NRNFKGRQGS PSGRTLLMSP AMVAAAAIAG EVTDVRAFL 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08461.1.
RefSeqNP_681699.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DKF0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr0909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08461; BAC08461; BAC08461.
GeneID1011413.
KEGGtel:tlr0909.
PATRIC23927110. VBITheElo119873_0955.

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01703.
OMAQARAKTM.
OrthoDBEOG600DP5.

Enzyme and pathway databases

UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPMF_01026. LeuC_type1.
InterProIPR004430. 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]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF53732. SSF53732. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_THEEB
AccessionPrimary (citable) accession number: Q8DKF0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways