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M5E1P8 · M5E1P8_9FIRM

Function

function

Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site15[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site45(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site45dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site45isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site77(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site77dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site77isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site99[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site127(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site127dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site127isopentenyl diphosphate (UniProtKB | ChEBI)
Active site129Proton donor
Binding site165(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site193[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site221(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site221dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site221isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site223(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site223dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site223isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site265(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site265dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site265isopentenyl diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentribosome
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Function4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity
Molecular Functionmetal ion binding
Molecular Functionnucleic acid binding
Biological Processdimethylallyl diphosphate biosynthetic process
Biological Processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Biological Processterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-hydroxy-3-methylbut-2-enyl diphosphate reductase
  • EC number
  • Short names
    HMBPP reductase

Gene names

    • Name
      ispH
    • ORF names
      HSACCH_01367

Organism names

Accessions

  • Primary accession
    M5E1P8

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region283-363Disordered
Compositional bias295-358Acidic residues
Domain371-440S1 motif
Domain458-523S1 motif
Domain544-612S1 motif
Domain629-698S1 motif
Region698-753Disordered
Compositional bias710-740Polar residues

Sequence similarities

Belongs to the IspH family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    753
  • Mass (Da)
    83,313
  • Last updated
    2013-05-29 v1
  • MD5 Checksum
    17FD242AAAFA216DB6F4E58DE605432E
MKVLEVITAEEAGFCFGVERAIEMVLEAAGENEEINVYTLGPLIHNPQVVEKLEDKNVKVASSLADIDSGIVIIRSHGVAPEVIEEAREKNLKIIDATCPFVKNAQKYAKQLVDEGYQTFIYGDGDHPEVHGIYGASDKKAIIIRDKEDLKSVELKSRIGFVAQTTKSPESFRDIISLVATKVKELKVFNTICNTTDVRQSSAKKLAEDVDIMFVIGGHNSANTTRLAEICTATNTPTYHIETAAEIDKKWLSGKNKVGITAGASTPDWLIREVVQLMNEENKEVNVESTENVEEKEEQVVEEVEEKVEETEETTEVTEETTDEKEADNSEEAVEESAEEEEAEASEDTAETEEEAEFKYSDNDIADLRKGQKVTGTVVEINDNGVYVDVNYKTDGFIPLRHLSHRTVEDAHDIVSMDDEIEVVILTLEDDEGNMILSKKQADYEQAWEKIVEAHENDEIIEAEVTKEVKGGLVVDVGVRGFIPASHVAIGYVDDLSDYVGETLRLKVIEVERDNNNVVLSAKKVLEKERAAKKDETLAALEEGQTVEGTVTKLVDFGAFIDLGGIEGLLHISEMSWGRIESPSEVLSEGEKVEVKVLGVNKEEERISLGLKQLLPDPWEEFADKHYEGEVIEGKITKLVDFGAFMEVEKGIEGLIHISQLSHRHVKTADEVVNVGDKREAKIINIDADQERVGLSLKELEEKPEPKQESSSSSKSSNQSRSSKSKSSNNDDSSSSGGATIREIVGDIFDQGE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias295-358Acidic residues
Compositional bias710-740Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAUI01000015
EMBL· GenBank· DDBJ
CCU79483.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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