D1CBE5 · D1CBE5_THET1

Function

function

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

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 site22GTP (UniProtKB | ChEBI)
Binding site29[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site33[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site35S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site36[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site72GTP (UniProtKB | ChEBI)
Binding site76S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site103GTP (UniProtKB | ChEBI)
Binding site127S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site165GTP (UniProtKB | ChEBI)
Binding site199S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site262[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site265[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site267-269GTP (UniProtKB | ChEBI)
Binding site279[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
    • Ordered locus names
      Tter_1202

Organism names

Accessions

  • Primary accession
    D1CBE5

Proteomes

Interaction

Subunit

Monomer and homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-228Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    335
  • Mass (Da)
    38,149
  • Last updated
    2010-01-19 v1
  • Checksum
    C3AACC125466F152
MSFNHHPQKFIDSFGRHIEDLRISVIDKCNFRCTYCMPAEGLPWLKKSELLTFDEIERLVRISVERGIKSVRVTGGEPTVRAGLPELIHRLVNIPGLEDVSLTTNGFLLRKMAKDLAEAGLTRINVSLDTLVREKFQHITRRDHLSEVLAGLEELEKYPSIRPIKINTVAIRGFTEPEVLDFARLARRKPYVVRFIEFMPLDADQTWSPDKILTGREIFEMINAVYPLVPVDTDPSSTSRVYRFADGKGEIGFINPVSEPFCSTCNRIRITADGQLRTCLFSTWETDLRTPLRSGMSDDQIGEIMLQAIKKKEMKHKINEPGFVRASRTMSQIGG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001825
EMBL· GenBank· DDBJ
ACZ42110.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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