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Q9EVG8 (LEUC_BUCUM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Encoded onPlasmid pLeu (pBAp1)
OrganismBuchnera aphidicola subsp. Uroleucon ambrosiae
Taxonomic identifier118117 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length444 AA.
Sequence statusFragment.
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.

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.

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 – ›444›4443-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
PRO_0000076724

Sites

Metal binding3481Iron-sulfur (4Fe-4S) By similarity
Metal binding4081Iron-sulfur (4Fe-4S) By similarity
Metal binding4111Iron-sulfur (4Fe-4S) By similarity

Natural variations

Natural variant22 – 232GE → RG in strain: GA2181.
Natural variant471S → N in strain: MNb027.
Natural variant2541L → F in strain: UT.002.
Natural variant3121N → K in strain: OH.036.
Natural variant3151L → V in strain: GA2181, MNb027, OH.036 and UT.002.
Natural variant3391S → A in strain: UT.002.

Experimental info

Sequence conflict4281T → H in AAG31397. Ref.1
Non-terminal residue4441

Sequences

Sequence LengthMass (Da)Tools
Q9EVG8 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: CEA7649DEAEB38EA

FASTA44449,593
        10         20         30         40         50         60 
MTSKTLYQKI YDSHVVYEDK NGESILYIDL HLLHEVTSPQ AFDALRSKKR KVRQSKKTFA 

        70         80         90        100        110        120 
TMDHNVSTKI QSISASGSMA KKQMEQLIKN CRDFNIPLYD INNPNQGIVH VIAPEKGMTL 

       130        140        150        160        170        180 
PGMTIVCGDS HTSTHGAFGA LAFGIGTSEV EHVLATQTLK QKRFKNMKVE IIGKIPKFVT 

       190        200        210        220        230        240 
AKDIILFIIG QLGSSSGTGY VIEFCGDVIK NISMEERMTI CNMAIEMGAK SGLIAPDEIT 

       250        260        270        280        290        300 
YKYLKDKIYS PSGLFWEKSL DYWKFLKSDK NAHFDKCITL DISNLAPQIT WGTNPDQVIS 

       310        320        330        340        350        360 
IDEKIPDYNN INSLLKKESA KSACEYMGLK SNTYLTNISI DRVFIGSCTN ARIEDLRAAS 

       370        380        390        400        410        420 
KILKNRKIAK HVKAIVVPGS GSVKRKAEQE GLDKIFIDSG FEWRLPGCSM CLGMNKDRLN 

       430        440 
FGERCASTSN RNFEGRQGRG GRTH

« Hide

References

[1]"Vertical transmission of biosynthetic plasmids in aphid endosymbionts (Buchnera)."
Wernegreen J.J., Moran N.A.
J. Bacteriol. 183:785-790(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Intraspecific variation in symbiont genomes: bottlenecks and the aphid-Buchnera association."
Funk D.J., Wernegreen J.J., Moran N.A.
Genetics 157:477-489(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-436.
Strain: AL.012, AZ.026, AZ.180, DC.005, GA.039, GA2181, IL.014, IL2.17, IN.018, KY.172, KY2.37, LA.013, MI.035, MN.001, MNb027, MS.040, NY.016, OH.036, TN.173, TN2.38, UT.002 and VA.015.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF197454 Genomic DNA. Translation: AAG31397.1.
AF196404 Genomic DNA. Translation: AAK21726.1.
AF196407 Genomic DNA. Translation: AAK21731.1.
AF196408 Genomic DNA. Translation: AAK21733.1.
AF196409 Genomic DNA. Translation: AAK21735.1.
AF196410 Genomic DNA. Translation: AAK21737.1.
AF196412 Genomic DNA. Translation: AAK21741.1.
AF196413 Genomic DNA. Translation: AAK21743.1.
AF196414 Genomic DNA. Translation: AAK21745.1.
AF196415 Genomic DNA. Translation: AAK21747.1.
AF196417 Genomic DNA. Translation: AAK21751.1.
AF196418 Genomic DNA. Translation: AAK21753.1.
AF196419 Genomic DNA. Translation: AAK21755.1.
AF196420 Genomic DNA. Translation: AAK21757.1.
AF196421 Genomic DNA. Translation: AAK21759.1.
AF196422 Genomic DNA. Translation: AAK21761.1.
AF196423 Genomic DNA. Translation: AAK21763.1.
AF196424 Genomic DNA. Translation: AAK21765.1.
AF196402 Genomic DNA. Translation: AAK21723.1.
AF196406 Genomic DNA. Translation: AAK21729.1.
AF196416 Genomic DNA. Translation: AAK21749.1.
AF196425 Genomic DNA. Translation: AAK21767.1.
AF196411 Genomic DNA. Translation: AAK21739.1.

3D structure databases

ProteinModelPortalQ9EVG8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 3 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. Aconitase_N. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEUC_BUCUM
AccessionPrimary (citable) accession number: Q9EVG8
Secondary accession number(s): Q99Q73 expand/collapse secondary AC list , Q99QQ9, Q9AJ47, Q9AJ48, Q9AJ49, Q9AJ50, Q9AJ52
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: April 3, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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