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Q9V1I9 (LEUD2_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 68. 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 2

EC=4.2.1.33
Alternative name(s):
Alpha-IPM isomerase 2
Short name=IPMI 2
Isopropylmalate isomerase 2
Gene names
Name:leuD2
Synonyms:leuD-2
Ordered Locus Names:PYRAB04380
ORF Names:PAB0288
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length163 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. HAMAP MF_01032

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01032

(2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP MF_01032

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP MF_01032

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP MF_01032

Sequence similarities

Belongs to the LeuD family. LeuD type 2 subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1631633-isopropylmalate dehydratase small subunit 2 HAMAP MF_01032
PRO_0000141945

Sequences

Sequence LengthMass (Da)Tools
Q9V1I9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F759C5473A36B632

FASTA16318,010
        10         20         30         40         50         60 
MITTGRVWKF WDNVSTDEIT PGRYNLTKDP QELARIAFIE VRPEFAEKVR RGDVVVGGKN 

        70         80         90        100        110        120 
FGIGSSRESA ALALKAAGVS GIIAKSFGRI FYRNAVNLGI PLLIGDTDEL EDGDVITVNW 

       130        140        150        160 
ETGEVRKNGQ TLQFEPLPGF LLEIVREGGI LEFIRRRGDL CIG 

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49360.1.
PIRA75160.
RefSeqNP_126129.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V1I9.
SMRQ9V1I9. Positions 1-162.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000002332; EBPYRP00000002263; EBPYRG00000002332.
GeneID1495332.
GenomeReviewsGene locus PYRAB04380 in contig AL096836_GR.
KEGGpab:PAB0288.
NMPDRfig|272844.1.peg.456.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022453.
HOGENOMHBG304838.
OMAITPGRYN.
PhylomeDBQ9V1I9.
ProtClustDBPRK00439.

Enzyme and pathway databases

BioCycPABY272844:PAB0288-MONOMER.

Family and domain databases

HAMAPMF_01032. LeuD_type2.
[Tree]
InterProIPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR011827. IsopropMal_deHydtase_ssu.
[Graphical view]
Gene3DG3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
KOK01704.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PfamPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
TIGRFAMsTIGR02087. LEUD_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLEUD2_PYRAB
AccessionPrimary (citable) accession number: Q9V1I9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 68 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