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Links from Protein

Items: 11

1.

Molybdopterin oxidoreductase N-terminal domain

This is the N-terminal domain of Pfam:PF00384 found in a number of molybdopterin-containing oxidoreductases such as dimethyl sulfoxide/trimethylamine N-oxide reductase, also known as DMSO reductase (EC:1.7.2.3, EC:1.8.5.3) [1]. [1]. 10835270. Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site. Stewart LJ, Bailey S, Bennett B, Charnock JM, Garner CD, McAlpine AS;. J Mol Biol. 2000;299:593-600. (from Pfam)

Date:
2024-10-16
Family Accession:
NF036859.5
Method:
HMM
2.

molybdopterin dinucleotide binding domain-containing protein

This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyses the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor [1]. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules [2]. [1]. 9818358. The formylmethanofuran dehydrogenase isoenzymes in Methanobacterium wolfei and Methanobacterium thermoautotrophicum: induction of the molybdenum isoenzyme by molybdate and constitutive synthesis of the tungsten isoenzyme. Hochheimer A, Hedderich R, Thauer RK;. Arch Microbiol 1998;170:389-393. [2]. 8890912. Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 A resolution. Schneider F, Lowe J, Huber R, Schindelin H, Kisker C, Knablein J;. J Mol Biol 1996;263:53-69. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
molybdopterin cofactor binding (GO:0043546)
Date:
2024-10-16
Family Accession:
NF013717.5
Method:
HMM
3.

molybdopterin-dependent oxidoreductase

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-08-14
Family Accession:
NF012602.5
Method:
HMM
4.
new record, indexing in progress
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5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.

molybdopterin guanine dinucleotide-containing S/N-oxide reductase

molybdopterin guanine dinucleotide-containing S/N-oxide reductase similar to dimethyl sulfoxide/trimethylamine N-oxide reductase that catalyzes the reduction of dimethyl sulfoxide (DMSO) and trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and trimethylamine, respectively

Date:
2020-07-24
Family Accession:
11489210
Method:
Sparcle
11.

molybdopterin guanine dinucleotide-containing S/N-oxide reductase

This enzyme family shares sequence similarity and a requirement for a molydenum cofactor as the only prosthetic group. The form of the cofactor is a single molybdenum atom coordinated by two molybdopterin guanine dinucleotide molecules. Members of the family include biotin sulfoxide reductase, dimethylsulfoxide reductase, and trimethylamine-N-oxide reductase, although a single member may show all those activities and related activities; it may not be possible to resolve the primary function for members of this family by sequence comparison alone. A number of similar molybdoproteins in which the N-terminal region contains a CXXXC motif and may bind an iron-sulfur cluster are excluded from this set, including formate dehydrogenases and nitrate reductases. Also excluded is the A chain of a heteromeric, anaerobic DMSO reductase, which also contains the CXXXC motif.

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Molecular Function:
molybdopterin cofactor binding (GO:0043546)
Date:
2022-03-28
Family Accession:
TIGR00509.1
Method:
HMM
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