MOCOS 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. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 2.8.1.9; Lyase
Chromosomal Location of human Ortholog: 18q12.2
Cellular Component:  cytosol
Molecular Function:  lyase activity; Mo-molybdopterin cofactor sulfurase activity; molybdenum cofactor sulfurtransferase activity; molybdenum ion binding; protein binding; pyridoxal phosphate binding
Biological Process:  Mo-molybdopterin cofactor biosynthetic process; molybdopterin cofactor biosynthetic process; molybdopterin cofactor metabolic process
Disease: Xanthinuria, Type Ii
Reference #:  Q96EN8 (UniProtKB)
Alt. Names/Synonyms: FLJ20733; HMCS; MCS; MoCo sulfurase; MOCOS; Molybdenum cofactor sulfurase; Molybdenum cofactor sulfurtransferase; MOS
Gene Symbols: MOCOS
Molecular weight: 98,120 Da
Basal Isoelectric point: 6.23  Predict pI for various phosphorylation states
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MOCOS

Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB