A0A1E7PUH3 · A0A1E7PUH3_9GAMM

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 site18GTP (UniProtKB | ChEBI)
Binding site25[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site29[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site31S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site32[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site67GTP (UniProtKB | ChEBI)
Binding site71S-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 site256[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site259[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site261-263GTP (UniProtKB | ChEBI)
Binding site273[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
      BG841_02945

Organism names

  • Taxonomic identifier
  • Strain
    • X15-166B
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Marinobacteraceae > Marinobacter

Accessions

  • Primary accession
    A0A1E7PUH3

Proteomes

Interaction

Subunit

Monomer and homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-225Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    330
  • Mass (Da)
    37,326
  • Last updated
    2017-01-18 v1
  • MD5 Checksum
    164EDDA425B7C677FD8DAB30A95EDE89
MPKAPLTDRFGRTIDYVRLSVTDRCDFRCVYCMSEDMTFLPRKQVLTLEEIARLARTFKSLGTEKIRLTGGEPLVRKDIVGLVEEIGALGLRDFAMTTNGNQLTRLAEPLRQAGLHRLNISLDTLDAERFRTITRTGNLQRVLDGLDAARDAGFKRLKLNTVIMKGRNDDEVTELVEFARAKQVDISFIEEMPLGEITAHDRGESLCSSDEVRALIEQRHELLPTTDDTGGPARYYRMADSPIRVGFISPHSHNFCATCNRVRVTVEGRLLLCLGNEHSVDLRRVLRGYPEDDGHLRQAIIDAMDLKPERHHFSSEGEVQILRFMNMTGG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MEIY01000001
EMBL· GenBank· DDBJ
OEY65516.1
EMBL· GenBank· DDBJ
Genomic DNA

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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