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 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
      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

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp