MOCOS
entrez
55034
canonical
uniprot
Q96EN8
canonical
ensembl
ENSG00000075643
resolver
ensp
ENSP00000261326
resolver
enst
ENST00000261326
resolver
genesymbol
MOCOS
resolver
hgnc
HGNC:18234
resolver
uniprot
Q53GP5
resolver
uniprot
Q8N3A4
resolver
uniprot
Q9NWM7
resolver
uniprot_entry
MOCOS_HUMAN
resolver
uniprot_sec
Q53GP5
resolver
uniprot_sec
Q8N3A4
resolver
uniprot_sec
Q9NWM7
resolver
amino_acid_sequence
MAGAAAESGRELWTFAGSRDPSAPRLAYGYGPGSLRELRAREFSRLAGTVYLDHAGATLFSQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHFHTTAEDYTVIFTAGSTAALKLVAEAFPWVSQGPESSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEDLWSAEERSASASNPDCQLPHLFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAASYVSTSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLAGEDFYIPRQSVAQRFEDGTISFLDVIALKHGFDTLERLTGGMENIKQHTFTLAQYTYVALSSLQYPNGAPVVRIYSDSEFSSPEVQGPIINFNVLDDKGNIIGYSQVDKMASLYNIHLRTGCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQAFLRFIIDTRLHSSGDWPVPQAHADTGETGAPSADSQADVIPAVMGRRSLSPQEDALTGSRVWNNSSTVNAVPVAPPVCDVARTQPTPSEKAAGVLEGALGPHVVTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRIMVIKAKGMEPIEVPLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHGKDQLPGTMATLSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFSLKDLSLRFRANIIINGKRAFEEEKWDEISIGSLRFQVLGPCHRCQMICIDQQTGQRNQHVFQKLSESRETKVNFGMYLMHASLDLSSPCFLSVGSQVLPVLKENVEGHDLPASEKHQDVTS
uniprot
proteins
disease_involvement
DISEASE: Xanthinuria 2 (XAN2) [MIM:603592]: A disorder characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. In addition, XAN2 patients cannot metabolize allopurinol into oxypurinol due to dual deficiency of xanthine dehydrogenase and aldehyde oxidase. {ECO:0000269|PubMed:11302742, ECO:0000269|PubMed:14624414, ECO:0000269|PubMed:17368066, ECO:0000269|PubMed:29935280, ECO:0000269|PubMed:34356852, ECO:0000269|Ref.12}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.8.1.9
uniprot
proteins
function
FUNCTION: Sulfurates the molybdenum cofactor (PubMed:34356852). 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 (PubMed:34356852). In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime (PubMed:16973608). {ECO:0000255|HAMAP-Rule:MF_03050, ECO:0000269|PubMed:16973608, ECO:0000269|PubMed:34356852}.
uniprot
proteins
mass_dalton
98120
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000269|PubMed:34356852}.
uniprot
proteins
protein_family
Class-V pyridoxal-phosphate-dependent aminotransferase family
uniprot
proteins
protein_family
MOCOS subfamily
uniprot
proteins
pubmed
11302742
uniprot
proteins
pubmed
14624414
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16177791
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
16973608
uniprot
proteins
pubmed
17368066
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29935280
uniprot
proteins
pubmed
34356852
uniprot
proteins
sequence_length
888
uniprot
proteins