SMART: Pfam domain MOSC

The domain within your query sequence starts at position 205 and ends at position 338; the E-value for the MOSC domain shown below is 1.1e-28.

SQNNEVAYSDASPFLVLSEASLEDLNSRLERRVKATNFRPNIVISGCGVYAEDSWNEVLI
GDVELKRVMACTRCLLTTVDPDTGISDRKEPLETLKSYRLCDPSEQALYGKLPIFGQYFA
LENPGTIRVGDPVY

MOSC

PFAM accession number:	PF03473
Interpro abstract (IPR005302):	Molybdenum cofactor (MOCO) sulphurases [ (PUBMED:16784786) ] catalyse the insertion of a terminal sulphur ligand into the molybdenum cofactor, thereby converting the oxo form of MOCO to a sulphurylated form. Suphurylated MOCO is required by several enzymes, including: aldehyde oxidase ( EC 1.2.3.1 ), which function in the last step of abscisic acid biosynthesis in plants [ (PUBMED:11549764) ]; and xanthine dehydrogenase ( EC 1.17.1.4 ), which synthesis uric acid from xanthine during nitrogen metabolism [ (PUBMED:12650690) ]. This entry represents the beta-barrel C-terminal domain of MOCO sulphurase (MOSC domain), which has a beta-barrel structure similar to that of the beta-barrel domain in pyruvate kinase and contains a highly conserved cysteine residue required for activity. MOSC domains are found in several diverse metal-sulphur cluster biosynthesis proteins from both eukaryotes and prokaryotes. MOSC domains occu as either stand-alone forms, such as the YiiM protein from Escherichia coli, or fused to other domains, such as a NifS-like catalytic domain in MOCO sulphurase. The MOSC domain is predicted to be a sulphur-carrier domain that receives sulphur abstracted from pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulphur-metal clusters [ (PUBMED:11886751) ]. The MOSC domain contains several patches of hydrophobic residues and an absolutely conserved cysteine residue situated closer to the C-terminal end of the domain. The absolutely conserved cysteine in the MOSC domain is reminiscent of the analogous conservation of a cysteine in the active site of the thioredoxin and rhodanese superfamilies. Members of both these superfamilies, especially of the latter one, have been implicated in the synthesis of Fe-S clusters, through mobilisation of sulphur with their active cysteine.
GO function:	molybdenum ion binding (GO:0030151), catalytic activity (GO:0003824), pyridoxal phosphate binding (GO:0030170)

PFAM accession number:

PF03473

Interpro abstract (IPR005302):

Molybdenum cofactor (MOCO) sulphurases [ (PUBMED:16784786) ] catalyse the insertion of a terminal sulphur ligand into the molybdenum cofactor, thereby converting the oxo form of MOCO to a sulphurylated form. Suphurylated MOCO is required by several enzymes, including: aldehyde oxidase ( EC 1.2.3.1 ), which function in the last step of abscisic acid biosynthesis in plants [ (PUBMED:11549764) ]; and xanthine dehydrogenase ( EC 1.17.1.4 ), which synthesis uric acid from xanthine during nitrogen metabolism [ (PUBMED:12650690) ].

This entry represents the beta-barrel C-terminal domain of MOCO sulphurase (MOSC domain), which has a beta-barrel structure similar to that of the beta-barrel domain in pyruvate kinase and contains a highly conserved cysteine residue required for activity. MOSC domains are found in several diverse metal-sulphur cluster biosynthesis proteins from both eukaryotes and prokaryotes. MOSC domains occu as either stand-alone forms, such as the YiiM protein from Escherichia coli, or fused to other domains, such as a NifS-like catalytic domain in MOCO sulphurase. The MOSC domain is predicted to be a sulphur-carrier domain that receives sulphur abstracted from pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulphur-metal clusters [ (PUBMED:11886751) ].

The MOSC domain contains several patches of hydrophobic residues and an absolutely conserved cysteine residue situated closer to the C-terminal end of the domain. The absolutely conserved cysteine in the MOSC domain is reminiscent of the analogous conservation of a cysteine in the active site of the thioredoxin and rhodanese superfamilies. Members of both these superfamilies, especially of the latter one, have been implicated in the synthesis of Fe-S clusters, through mobilisation of sulphur with their active cysteine.

GO function:

molybdenum ion binding (GO:0030151), catalytic activity (GO:0003824), pyridoxal phosphate binding (GO:0030170)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry MOSC