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    Links from Protein

    Items: 9

    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:
    2017-05-22
    Family Accession:
    11485911
    Method:
    Sparcle
    8.

    UDP-N-acetylmuramate dehydrogenase

    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:
    NF010480.0
    Method:
    HMM
    9.

    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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