A0A351IU65 · A0A351IU65_9ACTN

Function

function

Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.

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 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site17GTP (UniProtKB | ChEBI)
Binding site24[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site28[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site30S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site31[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site68GTP (UniProtKB | ChEBI)
Binding site72S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site97GTP (UniProtKB | ChEBI)
Binding site121S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site158GTP (UniProtKB | ChEBI)
Binding site192S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site254[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site257[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site259-261GTP (UniProtKB | ChEBI)
Binding site271[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functioncyclic pyranopterin monophosphate synthase activity
Molecular FunctionGTP 3',8'-cyclase activity
Molecular FunctionGTP binding
Molecular Functionmetal ion binding
Molecular FunctionS-adenosyl-L-methionine binding
Biological ProcessMo-molybdopterin cofactor biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    GTP 3',8-cyclase
  • EC number
  • Alternative names
    • Molybdenum cofactor biosynthesis protein A

Gene names

    • Name
      moaA
    • ORF names
      DCY87_02305

Organism names

  • Taxonomic identifier
  • Strain
    • UBA11106
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Acidimicrobiia > Acidimicrobiales > Acidimicrobiaceae

Accessions

  • Primary accession
    A0A351IU65

Proteomes

Interaction

Subunit

Monomer and homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-222Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    327
  • Mass (Da)
    36,037
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    16E347B1F6456D50C9CE2F596001FD03
MARQLIDTFGRVHRDLRISVTDRCSFRCTYCMPAEGLEWLPREELLTFEEIERVARLMVERHGVESIRLTGGEPTVRASLSTLVGMLADLPVDLTMTTNGVTLRALAGDLAAAGLKRINISLDSLHVDRFVELTRRDNLGRVLDGIDAAIEAGLDPVKVNVVVMRGVNDDEIVDLARFGRERGVEVRFIEFMPLDADRSWSDGAVVGCDEIVARIAEVFPLEPVDRTSAPATRYRYLDGAGCFGVVASVTRSFCDTCDRIRLTADGQFRNCLFAVEEFDLRSLLRSGASDEDLSELLQGAVAAKWAGHGISSVDFIRPNRSMSQIGG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNIH01000098
EMBL· GenBank· DDBJ
HAZ17585.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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