A0A150IHU7 · A0A150IHU7_9EURY

Function

function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site298[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site358[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site361[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function3-isopropylmalate dehydratase activity
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionisomerase activity
Molecular Functionmetal ion binding
Biological ProcessL-leucine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3-isopropylmalate dehydratase large subunit
  • EC number
  • Alternative names
    • Alpha-IPM isomerase
      (IPMI
      )
    • Isopropylmalate isomerase

Gene names

    • Name
      leuC_2
    • Synonyms
      leuC
    • ORF names
      APG10_01607
      , APG11_00404
      , APG12_01733

Organism names

  • Taxonomic identifier
  • Strains
    • B03fssc0709_Meth_Bin005
    • B15fssc0709_Meth_Bin003
    • BMIXfssc0709_Meth_Bin006
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Candidatus Methanofastidiosia > Candidatus Methanofastidiosales > Candidatus Methanofastidiosaceae > Candidatus Methanofastidiosum

Accessions

  • Primary accession
    A0A150IHU7
  • Secondary accessions
    • A0A150ITP7
    • A0A150IVE6

Proteomes

Interaction

Subunit

Heterodimer of LeuC and LeuD.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain19-284Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha
Domain286-409Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha

Sequence similarities

Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    418
  • Mass (Da)
    45,277
  • Last updated
    2016-06-08 v1
  • Checksum
    D63CFB46BD77D31A
MGKTISEKIIGNKAGATVEAGQIVEANVDYVMVNDVTGLPAFEQFEKLPKGTMPLKEKIVLIPDHYVPNKDVASAEQAKRMREFAKKYEIKNYFEVGRGGVCHQLMIEKGFVAPGRLIVGADSHTCSYGALGAFSTGIGSTEAAAVMAIGKLWLKVPDSIKITVNGKLDNYVYGKDIILHVIGDIGVEGALYKAMEYYGNTIENLSLSDRISISNMAIEAGGKAGIIPPDDKVFEYLQERIKGNYNPVYSDKDAYYIEDLKYDAADIPPTVSKPFLPSNTAPASEVDVKIDQAYLGSCTNGRIEDLRIAAEILKGRKINPEVRMLVVPASKEVFNQALKEGLIDIFEKADCFVCGPTCGACLGGYMGILADGEKCVATTNRNFIGRMGHKNSEVYLANPAVVAASALEGRIVDPREVL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LNGE01000054
EMBL· GenBank· DDBJ
KYC44583.1
EMBL· GenBank· DDBJ
Genomic DNA
LNGF01000006
EMBL· GenBank· DDBJ
KYC48391.1
EMBL· GenBank· DDBJ
Genomic DNA
LNJC01000053
EMBL· GenBank· DDBJ
KYC48991.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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