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Items: 8

1.

Mo-co oxidoreductase dimerisation domain

This domain is found in molybdopterin cofactor (Mo-co) oxidoreductases. It is involved in dimer formation, and has an Ig-fold structure [1]. [1]. 9428520. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC;. Cell 1997;91:973-983. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
molybdenum ion binding (GO:0030151)
Date:
2024-10-16
Family Accession:
NF015369.5
Method:
HMM
2.

molybdopterin-dependent oxidoreductase

This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity. [1]. 9428520. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC;. Cell 1997;91:973-983. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012401.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

sulfite dehydrogenase

sulfite dehydrogenase similar to Paracoccus pantotrophus SoxC, a component of the sulfur cycle SoxCD complex, which is involved in oxidation of sulfur compounds during chemolithothrophic growth; binds molybdopterin

Date:
2020-07-07
Family Accession:
11500462
Method:
Sparcle
8.

sulfite dehydrogenase

Members of this family are the sulfite dehydrogenase SoxC. All members have a twin-arginine translocation (TAT) signal for secretion of proteins with bound cofactor across the plasma membrane.

Gene:
soxC
GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
molybdenum ion binding (GO:0030151)
Date:
2021-09-22
Family Accession:
TIGR04555.1
Method:
HMM
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