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Entry version 64 (11 Dec 2019)
Sequence version 1 (01 Nov 1999)
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Protein

Monacolin J acid methylbutanoyltransferase

Gene

lovD

Organism
Aspergillus terreus
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acyltransferase that catalyzes the formation of lovastatin from monacolin J and LovF-bound 2-methylbutanoate. Can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor. Has broad substrate specificity and can utilize a variety of acyl donors and monacolin analogs (in vitro). Has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates. Can also catalyze the reverse reaction and function as hydrolase (in vitro).6 Publications

Miscellaneous

Directed evolution toward higher catalytic activity with free diketides led to an enzyme with 1000-fold higher activity in simvastatin synthesis, due to numerous mutations that affect protein folding and promote optimal alignment of the residues that are important for substrate binding and catalysis.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 0.62 min(-1) for simvastatin synthesis.
  1. KM=0.78 mM for monacolin J2 Publications
  2. KM=0.67 mM for alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lovastatin biosynthesis

    This protein is involved in the pathway lovastatin biosynthesis, which is part of Polyketide biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in the pathway lovastatin biosynthesis and in Polyketide biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei73Monacolin J1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei76Acyl-ester intermediate2 Publications1
    Binding sitei173Monacolin J1
    Binding sitei188Monacolin J1
    Binding sitei258Monacolin J1
    Binding sitei3662-methylbutanoate; via amide nitrogen1
    Binding sitei388Monacolin J1
    Binding sitei390Monacolin J1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Hydrolase, Transferase

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-18785

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00875

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Monacolin J acid methylbutanoyltransferase (EC:2.3.1.2383 Publications)
    Alternative name(s):
    Lovastatin hydrolase
    Simvastatin synthase LovD
    Short name:
    SV synthase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:lovD
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAspergillus terreus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri33178 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Catalyzes an important step in the biosynthesis of lovastatin, simvastatin and related compounds. Lovastatin and simvastatin are inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, a key enzyme in cholesterol biosynthesis, and are widely used to treat hypercholesteremia.4 Publications

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Loss of lovastatin biosynthesis.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4I → N: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi9A → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi12D → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with E-26; A-40; N-60; V-86; Y-161; T-190; S-275 and F-334. 1 Publication1
    Mutagenesisi26K → E: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 2 Publications1
    Mutagenesisi26K → E: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; A-40; N-60; V-86; Y-161; T-190; S-275 and F-334. 2 Publications1
    Mutagenesisi28R → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi35I → L: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi40C → A: Improves protein solubility upon overexpression in E.coli. Strongly improves protein solubility; when associated with N-60. Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; N-60; V-86; Y-161; T-190; S-275 and F-334. 1 Publication1
    Mutagenesisi43N → R: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi60C → A or N: Minor effect on protein solubility upon overexpression in E.coli. Strongly improves protein solubility; when associated with A-40. Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; V-86; Y-161; T-190; S-275 and F-334. 1 Publication1
    Mutagenesisi76S → A or N: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi86A → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; Y-161; T-190; S-275 and F-334. 1 Publication1
    Mutagenesisi96D → R: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi109S → C: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96;. 1 Publication1
    Mutagenesisi123A → P: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi157M → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi161H → Y: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; T-190; S-275 and F-334. 1 Publication1
    Mutagenesisi164S → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi172S → N: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; V-383; M-355; L-361; I-370; S-391 and K-404. 1 Publication1
    Mutagenesisi174L → F: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi178A → L: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi190A → T: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; Y-161; S-275 and F-334. 1 Publication1
    Mutagenesisi191N → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi192L → I: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; M-241; S-247; K-250; T-256; H-261; S-275; G-297; V-383; M-355; L-361; I-370; S-391 and K-404. 1 Publication1
    Mutagenesisi241Q → M: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi247A → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi250R → K: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; T-256; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi256S → T: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; H-261; S-275; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi261A → H: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; S-275; G-297; V-383; M-355; L-361; I-370; S-391 and K-404. 1 Publication1
    Mutagenesisi275G → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; G-297; M-355; L-361; I-370; V-383; S-391 and K-404. 2 Publications1
    Mutagenesisi275G → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; Y-161; T-190 and F-334. 2 Publications1
    Mutagenesisi297Q → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; M-355; L-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi334V → F: Strongly increases simvastatin synthase activity upon overexpression in E.coli; when associated with G-12; E-26; A-40; N-60; V-86; Y-161; T-190 and S-275. 1 Publication1
    Mutagenesisi355W → M: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-361; I-370; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi361L → M: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; V-383; G-297; M-355; I-370; S-391 and K-404. 1 Publication1
    Mutagenesisi370V → I: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; M-361; V-383; S-391 and K-404. 1 Publication1
    Mutagenesisi383A → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; L-361; I-370; S-391 and K-404. 1 Publication1
    Mutagenesisi391N → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; G-297; M-355; M-361; I-370; V-383 and K-404. 1 Publication1
    Mutagenesisi404H → K: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutanoate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96; C-109; P-123; V-157; G-164; N-172; F-174; L-178; G-191; I-192; M-241; S-247; K-250; T-256; H-261; S-275; V-383; G-297; M-355; M-361; I-370; V-383 and S-391. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004301001 – 413Monacolin J acid methylbutanoyltransferaseAdd BLAST413

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with LovF.

    2 Publications

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1413
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9Y7D1

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q9Y7D1

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the class-A beta-lactamase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410JB31 Eukaryota
    COG1680 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K20983

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.710.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001466 Beta-lactam-related
    IPR012338 Beta-lactam/transpept-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00144 Beta-lactamase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56601 SSF56601, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q9Y7D1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MGSIIDAAAA ADPVVLMETA FRKAVKSRQI PGAVIMARDC SGNLNYTRCF
    60 70 80 90 100
    GARTVRRDEC NQLPPLQVDT PCRLASATKL LTTIMALQCM ERGLVDLDET
    110 120 130 140 150
    VDRLLPDLSA MPVLEGFDDA GNARLRERRG KITLRHLLTH TSGLSYVFLH
    160 170 180 190 200
    PLLREYMAQG HLQSAEKFGI QSRLAPPAVN DPGAEWIYGA NLDWAGKLVE
    210 220 230 240 250
    RATGLDLEQY LQENICAPLG ITDMTFKLQQ RPDMLARRAD QTHRNSADGR
    260 270 280 290 300
    LRYDDSVYFR ADGEECFGGQ GVFSGPGSYM KVLHSLLKRD GLLLQPQTVD
    310 320 330 340 350
    LMFQPALEPR LEEQMNQHMD ASPHINYGGP MPMVLRRSFG LGGIIALEDL
    360 370 380 390 400
    DGENWRRKGS LTFGGGPNIV WQIDPKAGLC TLAFFQLEPW NDPVCRDLTR
    410
    TFEHAIYAQY QQG
    Length:413
    Mass (Da):46,037
    Last modified:November 1, 1999 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i731A140B6E609A24
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF141925 Genomic DNA Translation: AAD34555.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAD34555

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF141925 Genomic DNA Translation: AAD34555.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3HL9X-ray3.40A/B/C/D1-413[»]
    3HLBX-ray2.50A/B/C/D1-413[»]
    3HLCX-ray2.00A1-413[»]
    3HLDX-ray2.00A1-413[»]
    3HLEX-ray2.06A1-413[»]
    3HLFX-ray2.00A1-413[»]
    3HLGX-ray2.01A1-413[»]
    4LCLX-ray1.80A/B1-413[»]
    4LCMX-ray3.19A/B/C/D1-413[»]
    SMRiQ9Y7D1
    ModBaseiSearch...
    PDBe-KBiSearch...

    Genome annotation databases

    KEGGiag:AAD34555

    Phylogenomic databases

    eggNOGiENOG410JB31 Eukaryota
    COG1680 LUCA
    KOiK20983

    Enzyme and pathway databases

    UniPathwayiUPA00875
    BioCyciMetaCyc:MONOMER-18785

    Miscellaneous databases

    EvolutionaryTraceiQ9Y7D1

    Family and domain databases

    Gene3Di3.40.710.10, 1 hit
    InterProiView protein in InterPro
    IPR001466 Beta-lactam-related
    IPR012338 Beta-lactam/transpept-like
    PfamiView protein in Pfam
    PF00144 Beta-lactamase, 1 hit
    SUPFAMiSSF56601 SSF56601, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLOVD_ASPTE
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y7D1
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: November 1, 1999
    Last modified: December 11, 2019
    This is version 64 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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