MOCS3
entrez
27304
canonical
uniprot
O95396
canonical
ensembl
ENSG00000124217
resolver
ensp
ENSP00000244051
resolver
enst
ENST00000244051
resolver
genesymbol
MOCS3
resolver
genesymbol_syn
UBA4
resolver
hgnc
HGNC:15765
resolver
uniprot_entry
MOCS3_HUMAN
resolver
amino_acid_sequence
MASREEVLALQAEVAQREEELNSLKQKLASALLAEQEPQPERLVPVSPLPPKAALSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFRSIRLRSRRLDCAACGERPTVTDLLDYEAFCGSSATDKCRSLQLLSPEERVSVTDYKRLLDSGAFHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEAIWEEKQGTQEGAAVPIYVICKLGNDSQKAVKILQSLSAAQELDPLTVRDVVGGLMAWAAKIDGTFPQY
uniprot
proteins
disease_involvement
DISEASE: Molybdenum cofactor deficiency, type B2 (MOCODB2) [MIM:621373]: A form of molybdenum cofactor deficiency, an autosomal recessive metabolic disorder leading to the pleiotropic loss of molybdoenzyme activities. It is clinically characterized by neonatal or early-infantile onset of intractable seizures, poor feeding, psychomotor retardation, and facial dysmorphism associated with hypouricemia and elevated urinary sulfite levels. Affected individuals show severe neurologic damage and often die in early childhood. {ECO:0000269|PubMed:28544736, ECO:0000269|PubMed:33897766}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.7.80
uniprot
proteins
ec_number
2.8.1.11
uniprot
proteins
function
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln) (PubMed:19017811, PubMed:22453920, PubMed:30817134). Also essential during biosynthesis of the molybdenum cofactor (PubMed:15073332, PubMed:22453920, PubMed:30817134). Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A (PubMed:15073332, PubMed:19017811, PubMed:22453920). Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus (PubMed:19017811, PubMed:22453920). The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A (PubMed:15073332, PubMed:22453920). Subsequently, a transient disulfide bond is formed (PubMed:15073332, PubMed:22453920). Does not use thiosulfate as sulfur donor; NFS1 acting as a sulfur donor for thiocarboxylation reactions (PubMed:18650437, PubMed:22453920). {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:18650437, ECO:0000269|PubMed:19017811, ECO:0000269|PubMed:22453920, ECO:0000269|PubMed:30817134}.
uniprot
proteins
mass_dalton
49669
uniprot
proteins
mutagenesis
MUTAGEN 239; /note="C->A: Impairs sulfurtransferase activity."; /evidence="ECO:0000269|PubMed:15073332"; MUTAGEN 316; /note="C->A: Does not affect sulfurtransferase activity."; /evidence="ECO:0000269|PubMed:15073332"; MUTAGEN 324; /note="C->A: Does not affect sulfurtransferase activity."; /evidence="ECO:0000269|PubMed:15073332"; MUTAGEN 365; /note="C->A: Does not affect sulfurtransferase activity."; /evidence="ECO:0000269|PubMed:15073332"; MUTAGEN 412; /note="C->A: Abolishes sulfurtransferase activity."; /evidence="ECO:0000269|PubMed:15073332"; MUTAGEN 413; /note="K->R: Does not affect sulfurtransferase specificity and activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 414; /note="L->K: Does not affect sulfurtransferase specificity and activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 415; /note="G->A: Does not affect sulfurtransferase specificity and activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 416; /note="N->V: Does not affect sulfurtransferase specificity and activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 417; /note="D->R: Results in 470-fold increased activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 417; /note="D->T: Results in 90-fold increased activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 458; /note="P->G: Does not affect sulfurtransferase specificity and activity."; /evidence="ECO:0000269|PubMed:17459099"; MUTAGEN 460; /note="Y->A: Does not affect sulfurtransferase specificity and activity."; /evidence="ECO:0000269|PubMed:17459099
uniprot
proteins
pathway_participation
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
uniprot
proteins
protein_family
HesA/MoeB/ThiF family
uniprot
proteins
protein_family
UBA4 subfamily
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
15073332
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15910006
uniprot
proteins
pubmed
17459099
uniprot
proteins
pubmed
18650437
uniprot
proteins
pubmed
19017811
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22453920
uniprot
proteins
pubmed
23593335
uniprot
proteins
pubmed
28544736
uniprot
proteins
pubmed
30817134
uniprot
proteins
pubmed
33897766
uniprot
proteins
sequence_length
460
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:22453920, ECO:0000269|PubMed:23593335}.
uniprot
proteins