A5I365 · MOAA_CLOBH

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 site13GTP (UniProtKB | ChEBI)
Binding site20[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site24[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site26S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site27[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site63GTP (UniProtKB | ChEBI)
Binding site67S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site94GTP (UniProtKB | ChEBI)
Binding site118S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site155GTP (UniProtKB | ChEBI)
Binding site189S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site249[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site252[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site254-256GTP (UniProtKB | ChEBI)
Binding site266[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
      CBO1940, CLC_1885

Organism names

Accessions

  • Primary accession
    A5I365
  • Secondary accessions
    • A7G4M5

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000541861-319GTP 3',8-cyclase

Interaction

Subunit

Monomer and homodimer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-227Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    319
  • Mass (Da)
    36,402
  • Last updated
    2007-06-26 v1
  • Checksum
    1475CF50B29D90DF
MLDKHGRKINYLRVSVTDRCNLRCVYCMPPEGIVKKEHDNIMRYEEIFKVVKSASLLGVNKIRFTGGEPLILKDIDKLIYNTSKINSIKDIAMTTNAILLEDMVEELKKAGLKRVNISLDSLKEDRFKSITRGGDINKVFKSIEKSLSIGMKPIKINTVIMKGINDDEIDDFMNLTKKYPISVRFIELMPIGEGRKLYKDGYISSEEIISKHSDLIPVETEKSSTALLYKFKESKENIGFISPMSCKFCSGCNRVRLTSEGTLKPCLHSEKEVNLKNYVGNNQALLSKINETIYNKPLEHHMIEEKESKSKKMMYQIGG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000727
EMBL· GenBank· DDBJ
ABS38496.1
EMBL· GenBank· DDBJ
Genomic DNA
AM412317
EMBL· GenBank· DDBJ
CAL83482.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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