A0A6A7N4N6 · A0A6A7N4N6_9BURK

  • Protein
    Molybdenum cofactor guanylyltransferase
  • Gene
    mobA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site12-14GTP (UniProtKB | ChEBI)
Binding site25GTP (UniProtKB | ChEBI)
Binding site53GTP (UniProtKB | ChEBI)
Binding site73GTP (UniProtKB | ChEBI)
Binding site103GTP (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionGTP binding
Molecular Functionmetal ion binding
Molecular Functionmolybdenum cofactor guanylyltransferase activity
Molecular Functionmolybdopterin molybdotransferase activity
Biological ProcessMo-molybdopterin cofactor biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Molybdenum cofactor guanylyltransferase
  • EC number
  • Short names
    MoCo guanylyltransferase
  • Alternative names
    • GTP:molybdopterin guanylyltransferase
    • Mo-MPT guanylyltransferase
    • Molybdopterin guanylyltransferase
    • Molybdopterin-guanine dinucleotide synthase
      (MGD synthase
      )

Gene names

    • Name
      mobA
    • ORF names
      GEV02_17955

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FT29W
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Telluria group > Rugamonas

Accessions

  • Primary accession
    A0A6A7N4N6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain404-545MoaB/Mog

Domain

The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.

Sequence similarities

Belongs to the MobA family.
Belongs to the MoeA family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    633
  • Mass (Da)
    67,224
  • Last updated
    2020-06-17 v1
  • Checksum
    5CD52C308992D555
MSLKSKITGLILAGGRGTRMGRVDKGLQPFRGATLVEHVMRRLAPQVATVVINANRNLPQYQAVAGAAPVLPDYLDGFEGPLAGLQIGLQYCPTELLLTAPCDSPFLPDDLAERLHAALLEQNADVALAVTMEAEEGVEPYRQPHPVFALMKASLLPQLDTYLDTGARRMESWIKSLRVAEVMFDDADAFRNINTLAELQMHEQASASEPSAPVAPAVGDPGAMPVAEAQRIICERITPVTATETRALLHGALDRVLAEDIISPINVPAYDNSAMDGYALRGADLPAAGAPDATFKVIDIAYAGRPCTQTPQAGECIRIMTGAAIPPGCDSVLPQELASHIDGDSVTIPHGAIRTGANRRFAGEDLKAGGIALAKGKILRPADLGLVASLGIGEVTVQRKLRVAFFSTGDELRSLGDPLDDGCVYDSNRYTLFGMLTRLGCEVIDMGIVRDDPAALEAALRQACTKADAIITSGGVSEGAADYTRDIMARLGDVAFWKLAMRPGRPLAFGKIQTEADSAWLFGLPGNPVAVMVSFYMFARPALLRMMGAQATQPVMQARTTEAIRKRPGRTEYQRGILSTGAGGEPQVRLTGAQGSGILSSMTEANCIVVLREAQASIAAGEMVDVLLFDGLV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WHUG01000007
EMBL· GenBank· DDBJ
MQA40039.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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