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Links from Protein

Items: 10

1.

UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain

Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. [1]. 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:
UDP-N-acetylmuramate dehydrogenase activity (GO:0008762)
Date:
2024-10-16
Family Accession:
NF014872.5
Method:
HMM
2.

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
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.

UDP-N-acetylmuramate dehydrogenase

UDP-N-acetylmuramate dehydrogenase is responsible for the synthesis of UDP-N-acetylmuramic acid in bacterial cell wall biosynthesis

Date:
2022-10-19
Family Accession:
11477821
Method:
Sparcle
8.

UDP-N-acetylmuramate dehydrogenase

GO Terms:
Molecular Function:
UDP-N-acetylmuramate dehydrogenase activity (GO:0008762)
Molecular Function:
FAD binding (GO:0071949)
Date:
2021-08-12
Family Accession:
NF010478.0
Method:
HMM
9.

UDP-N-acetylmuramate dehydrogenase

Catalyzes the reduction of UDP-N-acetylglucosamine enolpyruvate to form UDP-N-acetylmuramate in peptidoglycan biosynthesis

Gene:
murB
GO Terms:
Molecular Function:
UDP-N-acetylmuramate dehydrogenase activity (GO:0008762)
Molecular Function:
FAD binding (GO:0071949)
Date:
2021-07-23
Family Accession:
NF000755.0
Method:
HMM
10.

UDP-N-acetylmuramate dehydrogenase

This HMM describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan.

Gene:
murB
GO Terms:
Molecular Function:
UDP-N-acetylmuramate dehydrogenase activity (GO:0008762)
Biological Process:
peptidoglycan biosynthetic process (GO:0009252)
Date:
2021-04-27
Family Accession:
TIGR00179.1
Method:
HMM
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