P9WJS3 · MOAA1_MYCTU

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 site30GTP (UniProtKB | ChEBI)
Binding site37[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site41[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site43S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site44[4Fe-4S] cluster 1 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site80GTP (UniProtKB | ChEBI)
Binding site84S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site115GTP (UniProtKB | ChEBI)
Binding site139S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site176GTP (UniProtKB | ChEBI)
Binding site210S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site273[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site276[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate
Binding site278-280GTP (UniProtKB | ChEBI)
Binding site290[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-substrate

GO annotations

AspectTerm
Cellular Componentplasma membrane
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 1
  • EC number
  • Alternative names
    • Molybdenum cofactor biosynthesis protein A 1

Gene names

    • Name
      moaA1
    • Synonyms
      moaA
    • ORF names
      MTCY164.19
    • Ordered locus names
      Rv3109

Organism names

Accessions

  • Primary accession
    P9WJS3
  • Secondary accessions
    • L0TEC9
    • O05786

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Miscellaneous

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001529761-359GTP 3',8-cyclase 1

Proteomic databases

Expression

Induction

Expression is positively regulated by the transcriptional regulator MoaR1.

Interaction

Subunit

Monomer and homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-241Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    359
  • Mass (Da)
    39,960
  • Last updated
    2014-04-16 v1
  • Checksum
    D6176DCBD467AE66
MSTPTLPDMVAPSPRVRVKDRCRRMMGDLRLSVIDQCNLRCRYCMPEEHYTWLPRQDLLSVKEISAIVDVFLSVGVSKVRITGGEPLIRPDLPEIVRTLSAKVGEDSGLRDLAITTNGVLLADRVDGLKAAGMKRITVSLDTLQPERFKAISQRNSHDKVIAGIKAVAAAGFTDTKIDTTVMRGANHDELADLIEFARTVNAEVRFIEYMDVGGATHWAWEKVFTKANMLESLEKRYGRIEPLPKHDTAPANRYALPDGTTFGIIASTTEPFCATCDRSRLTADGLWLHCLYAISGINLREPLRAGATHDDLVETVTTGWRRRTDRGAEQRLAQRERGVFLPLSTLKADPHLEMHTRGG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL123456
EMBL· GenBank· DDBJ
CCP45919.1
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