B7JWW6 · MOAA_RIPO1

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 site8GTP (UniProtKB | ChEBI)
Binding site15[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site19[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site21S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site22[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site60GTP (UniProtKB | ChEBI)
Binding site64S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site91GTP (UniProtKB | ChEBI)
Binding site115S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site155GTP (UniProtKB | ChEBI)
Binding site189S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site252[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site255[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site257-259GTP (UniProtKB | ChEBI)
Binding site269[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
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
      PCC8801_1769

Organism names

Accessions

  • Primary accession
    B7JWW6

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10001393171-329GTP 3',8-cyclase

Interaction

Subunit

Monomer and homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-229Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    329
  • Mass (Da)
    37,343
  • Last updated
    2009-02-10 v1
  • Checksum
    677E1CCAC078E3E7
MNPVDYLRISLIDRCNFRCQYCMPEGVKLDYILRSELLTDDELLTLIKAVFIPLGFTKFRLTGGEPLLRPGVVQLVRDIAALPQTEDLSMTTNGFLLSRMAKELYQAGLKRINISLDSLNQETFDKIIGNFGASKWQQTWEGIQTAYEVGFNPLKLNVVIIPGINEGEIEDLAALTIDRNWHVRFIEFMPIGNRELFSDRAWVPSEEIRQTIRQKWGLIESTIKGNGPADVFQIPGGKGTLGFISQMSECFCDRCNRMRLSADGWLRPCLLNETGQIDLKTALRQGIKTTELREQVREILAIKPNINYQERESGTQTGTYQRTMSQIGG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001287
EMBL· GenBank· DDBJ
ACK65815.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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