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B0KF82 (LEUD_PSEPG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 37. 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 small subunit

EC=4.2.1.33
Alternative name(s):
Alpha-IPM isomerase
Short name=IPMI
Isopropylmalate isomerase
Gene names
Name:leuD
Ordered Locus Names:PputGB1_1517
OrganismPseudomonas putida (strain GB-1) [Complete proteome] [HAMAP]
Taxonomic identifier76869 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length214 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_01031

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01031

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01031

Subunit structure

Heterodimer of LeuC and LeuD By similarity.

Sequence similarities

Belongs to the LeuD family. LeuD type 1 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2142143-isopropylmalate dehydratase small subunit HAMAP-Rule MF_01031
PRO_1000084260

Sequences

Sequence LengthMass (Da)Tools
B0KF82 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 200A415F6BEDB1DB

FASTA21424,225
        10         20         30         40         50         60 
MKAFTQHTGL VAPLDRANVD TDQIIPKQFL KSIKRTGFGP NLFDEWRYLD VGQPYQDNSK 

        70         80         90        100        110        120 
RPVNQEFVLN HARYQGASVL LARENFGCGS SREHAPWALD EYGFRSIIAP SFADIFFNNS 

       130        140        150        160        170        180 
FKNGLLPIIL SDEEVDELFK QVEANPGYQL TIDLQAQAVT RPDGKVLHFE IDAFRKHCLL 

       190        200        210 
NGLDDIGLTL QDSDAIKAFE GKHRAGQPWL FRDA 

« Hide

References

[1]"Complete sequence of Pseudomonas putida GB-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GB-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000926 Genomic DNA. Translation: ABY97422.1.
RefSeqYP_001667758.1. NC_010322.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING76869.PputGB1_1517.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY97422; ABY97422; PputGB1_1517.
GeneID5869293.
KEGGppg:PputGB1_1517.
PATRIC19930053. VBIPsePut76638_1529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0066.
HOGENOMHOG000222939.
KOK01704.
OMAYQDNSKR.
ProtClustDBPRK01641.

Enzyme and pathway databases

BioCycPPUT76869:GIXB-1564-MONOMER.
UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
HAMAPMF_01031. LeuD_type1.
InterProIPR004431. 3-IsopropMal_deHydase_ssu.
IPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF2. PTHR11670:SF2. 1 hit.
PfamPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
TIGRFAMsTIGR00171. leuD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLEUD_PSEPG
AccessionPrimary (citable) accession number: B0KF82
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: May 1, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families