Q2UH11 · MOCOS_ASPOR

Function

function

Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Features

Showing features for active site.

1822100200300400500600700800
TypeIDPosition(s)Description
Active site401

GO annotations

AspectTerm
Molecular Functionlyase activity
Molecular FunctionMo-molybdopterin cofactor sulfurase activity
Molecular Functionmolybdenum cofactor sulfurtransferase activity
Molecular Functionmolybdenum ion binding
Molecular Functionpyridoxal phosphate binding
Biological ProcessMo-molybdopterin cofactor biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Molybdenum cofactor sulfurase
  • EC number
  • Short names
    MCS
    ; MOS
    ; MoCo sulfurase
  • Alternative names
    • Molybdenum cofactor sulfurtransferase

Gene names

    • Name
      hxB
    • ORF names
      AO090023000633

Organism names

Accessions

  • Primary accession
    Q2UH11

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00002499621-822Molybdenum cofactor sulfurase
Modified residue239N6-(pyridoxal phosphate)lysine

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias633-648Polar residues
Region633-666Disordered
Domain643-820MOSC

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    822
  • Mass (Da)
    91,162
  • Last updated
    2013-10-16 v2
  • Checksum
    846EF95DC0255FFB
MQAKSKTESRAEYCTGYSEDVDVIREREYPFLKDTTYLDHAGTTLYPKSLIDSFARDLTSNLFGNPHSRSSSSQLSTQRIDDIRLRALRFFNADPDEFDLVFVANATAAIKLVVDVFRDSSPQGFWYGYFIDAHTSLVGAREIAERGHRCFLTSGEVERWIADLATDQKNFPRLFAYPGQSNLNGRRSPMQWCKKIRDGSSGAGNVYTLLDAASLVSTSPLDLSDASAAPDFTALSFYKIFGFPDLGALIVRKSAAGIIKKRKFFGGGTVDMVLAQGMPWHAKKSTIHECLEDGTLPFHNIIALDSALSTHGRLFGSMSNVSFHTRYLAKRLHNRLAAMTHFNGQKVCHLYMSPESDFDNSTQGPIIAFNIRNSSGAWIGKSEVERLANVKKIHIRSGSHCNSGGTATSLGWTGPELLRNFSAGLRCGDDHDVMDGRPTGILRVSLGAVSNLRDIDAFARFIDEFYIEKEPEFVSLVPPMEVVLQEPSFYVESLSVYPIKSCGAFKVPDGQRWEIKREGLAWDREWCLIHQGTGAALSMKKYPRMALIRPVIDLERGVLRITCGSDSKELEVSLRREITNLVTTSLCQSAKSSNVCGDRVVVQAYSSPTVASFFSNFLGVPCTLARFPPQISTRISNPTRSSRRSQRALMPGSFPEDPSPTSEQPPILLSNESPILLISRSSVNRLNENIKYNPRPSYSTPAKAVEADVFRANIVVAENLHQLANAERPYIEDTWESFSVGPEQLCFDVLGSCQRCQMVCVDPYTGTRREEPYSTLVKTRKINSKIVFGRHTSLSNMELSQGAGKPKSCTVMVGDVVTPQIA

Sequence caution

The sequence BAE59154.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias633-648Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BA000051
EMBL· GenBank· DDBJ
BAE59154.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

Genome annotation databases

Similar Proteins

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