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Links from Protein

Items: 13

1.

4Fe-4S dicluster domain-containing protein

This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024924.5
Method:
HMM
2.

4Fe-4S dicluster domain-containing protein

Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024581.5
Method:
HMM
3.

FAD-linked oxidase C-terminal domain-containing protein

This domain has a ferredoxin-like fold. [1]. 9141139. Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum. Mattevi A, Fraaije MW, Coda A, van Berkel WJ;. Proteins 1997;27:601-603. (from Pfam)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-10-16
Family Accession:
NF014910.5
Method:
HMM
4.

FAD-binding protein

This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [1]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan [2]. [1]. 9261083. Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity. Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ;. Structure 1997;5:907-920. [2]. 8805513. The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Benson TE, Walsh CT, Hogle JM;. Structure 1996;4:47-54. (from Pfam)

GO Terms:
Molecular Function:
flavin adenine dinucleotide binding (GO:0050660)
Date:
2024-10-16
Family Accession:
NF013714.5
Method:
HMM
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.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.

FAD-binding and (Fe-S)-binding domain-containing protein

FAD-binding and (Fe-S)-binding domain-containing protein, where the N-terminal FAD-binding and the C-terminal (Fe-S)-binding domains may function as oxidoreductases

Date:
2024-08-05
Family Accession:
11416044
Method:
Sparcle
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