A0A1W2FXB7 · A0A1W2FXB7_KIBAR

  • Protein
    Multifunctional fusion protein
  • Gene
    ispH
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
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.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster per subunit.
thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate 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.
Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-glyceraldehyde 3-phosphate and pyruvate: step 1/1.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site16[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 site78(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site78dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site78isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site100[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site128(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site128dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site128isopentenyl diphosphate (UniProtKB | ChEBI)
Active site130Proton donor
Binding site168(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site198[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site226(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site226dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site226isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site227(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site227dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site227isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site228(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site228dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site228isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site270(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI)
Binding site270dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site270isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site383thiamine diphosphate (UniProtKB | ChEBI)
Binding site424-426thiamine diphosphate (UniProtKB | ChEBI)
Binding site456Mg2+ (UniProtKB | ChEBI)
Binding site457-458thiamine diphosphate (UniProtKB | ChEBI)
Binding site485Mg2+ (UniProtKB | ChEBI)
Binding site485thiamine diphosphate (UniProtKB | ChEBI)
Binding site554thiamine diphosphate (UniProtKB | ChEBI)
Binding site635thiamine diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function1-deoxy-D-xylulose-5-phosphate synthase activity
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Function4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity
Molecular Functionmagnesium ion binding
Molecular Functionthiamine pyrophosphate binding
Biological Process1-deoxy-D-xylulose 5-phosphate biosynthetic process
Biological Processdimethylallyl diphosphate biosynthetic process
Biological Processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Biological Processterpenoid biosynthetic process
Biological Processthiamine biosynthetic process

Keywords

Enzyme and pathway databases

    • UPA00056UER00097
    • UPA00059UER00105
    • UPA00064UER00091

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    1-deoxy-D-xylulose-5-phosphate synthase
  • EC number
  • Alternative names
    • 1-deoxyxylulose-5-phosphate synthase
      (DXP synthase
      ; DXPS
      )
  • Recommended name
    4-hydroxy-3-methylbut-2-enyl diphosphate reductase
  • EC number
  • Short names
    HMBPP reductase

Gene names

    • Name
      ispH
    • Synonyms
      dxs
    • ORF names
      SAMN05661093_10096

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 43828
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Kibdelosporangium

Accessions

  • Primary accession
    A0A1W2FXB7

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain584-748Transketolase-like pyrimidine-binding

Sequence similarities

Belongs to the IspH family.
Belongs to the transketolase family. DXPS subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    906
  • Mass (Da)
    97,529
  • Last updated
    2017-06-07 v1
  • Checksum
    FC74DC973B6051B6
MTSKGKVVLAEPRGFCAGVHRAIAMTERALEMHGPPVYVRKQIVHNHYVVASLERRGARFVEEISEVPEGSVCVFSAHGVSPAVREAADQANLDVIDATCPLVSKVHQQAKRATRDGRLLLLIGHNNHEETEGTRGEVPERTIVVETVEDVDRLGLSPHTPVAYLTQTTLSVDDTAEVVARIRERFHDVAEPASDTICYASQNRQNGIKSLARQCELVLVVGSENSSNSQRMVDVARQAGARSYLVPDVGHLREEWLRDVRTVGVSSGASAPDVLVEQVLERLAEYGYGDVDVDITAVEDVVFSMPQRNHERLLPSVRQPSDLRRMSTPELTRLAGEIRTLLIEEVSRTGGHLGPSLGVVELTLGLHRVFDSPADRILWDTGHQAYVHKVLTGRWQDLGGLRTRDGLSGYPSQEESPHDFIENSHASTALSYAYGMSKADSLRGVTGRRVIAVVGDGSLTGGMAWEALNSIAGEGRPVVIVLNDNGRSYSPTVGGLARHLAGNEPDKFFTTLGLRYIGPVDGHDIDAVQNALREAASIDGPVVVHFLTRKGYGYELAENDQVDRFHAIKPMDPQTGVPVKASGRSWTSVFADELVRLGGLREDVVAITAAMQDPTGLSRFAERYPARVVDVGIAEQHAVTAAAGMAMAGMRPVVAIYSTFLNRAIDQVLLDVALHSCPVIFVLDRAGVTGDDGPSHNGMWDMSLLNVVPKMRIAAPRDAATLRSALRGALDTVDGPSTIRFPKGEVGDEVPAAFGCAGIDVLRPDPVDDVLLVSVGAMAKLCMEVAELLHSDGVGVTVVDPRWTKPVNPLLSAMAHRFKVVATVEDNVRVGGFGSLLGQQLQDANVTTPVVNFGIPQQFLAQGKRAEVLAECGLTAEVIAAEIVGRLLDPASWPAVEDVETSGLVG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FWXV01000015
EMBL· GenBank· DDBJ
SMD26513.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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