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Protein

Acyltransferase LovD

Gene

lovD

Organism
Aspergillus terreus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyltransferase that catalyzes the formation of lovastatin from monacolin J and LovF-bound 2-methylbutyrate. Can also convert monacolin J to simvastatin using alpha-dimethylbutyryl-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-methylbutyrate than with free diketide substrates. Can also catalyze the reverse reaction and function as hydrolase (in vitro).6 Publications

Catalytic activityi

Monacolin J acid + (S)-2-methylbutanoyl-[2-methylbutanoate polyketide synthase] = lovastatin acid + [2-methylbutanoate polyketide synthase].3 Publications

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-dimethylbutyryl-S-methyl-3-mercaptopropionate2 Publications

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731Monacolin J
    Active sitei76 – 761Acyl-ester intermediate2 Publications
    Binding sitei173 – 1731Monacolin J
    Binding sitei188 – 1881Monacolin J
    Binding sitei258 – 2581Monacolin J
    Binding sitei366 – 36612-methylbutyrate; via amide nitrogen
    Binding sitei388 – 3881Monacolin J
    Binding sitei390 – 3901Monacolin J

    GO - Molecular functioni

    • hydrolase activity Source: UniProtKB-KW
    • transferase activity, transferring acyl groups Source: UniProtKB

    GO - Biological processi

    • antibiotic biosynthetic process Source: UniProtKB
    • defense response to fungus Source: UniProtKB
    • polyketide biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Hydrolase, Transferase

    Enzyme and pathway databases

    UniPathwayiUPA00875.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyltransferase LovD (EC:2.3.1.2383 Publications)
    Alternative name(s):
    Lovastatin hydrolase
    Simvastatin synthase LovD
    Short name:
    SV synthase
    Gene namesi
    Name:lovD
    OrganismiAspergillus terreus
    Taxonomic identifieri33178 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Pathology & Biotechi

    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

    Disruption phenotypei

    Loss of lovastatin biosynthesis.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41I → N: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi9 – 91A → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi12 – 121D → 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 Publication
    Mutagenesisi26 – 261K → E: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publications
    Mutagenesisi26 – 261K → 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 Publications
    Mutagenesisi28 – 281R → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi35 – 351I → L: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi40 – 401C → 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 Publication
    Mutagenesisi43 – 431N → R: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi60 – 601C → 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 Publication
    Mutagenesisi76 – 761S → A or N: Abolishes enzyme activity. 1 Publication
    Mutagenesisi86 – 861A → 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 Publication
    Mutagenesisi96 – 961D → R: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi109 – 1091S → C: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; when associated with N-4; V-9; E-26; S-28; L-35; R-43; R-96;. 1 Publication
    Mutagenesisi123 – 1231A → P: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi157 – 1571M → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi161 – 1611H → 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 Publication
    Mutagenesisi164 – 1641S → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi172 – 1721S → N: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi174 – 1741L → F: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi178 – 1781A → L: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi190 – 1901A → 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 Publication
    Mutagenesisi191 – 1911N → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi192 – 1921L → I: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi241 – 2411Q → M: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi247 – 2471A → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi250 – 2501R → K: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi256 – 2561S → T: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi261 – 2611A → H: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi275 – 2751G → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publications
    Mutagenesisi275 – 2751G → 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 Publications
    Mutagenesisi297 – 2971Q → G: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi334 – 3341V → 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 Publication
    Mutagenesisi355 – 3551W → M: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi361 – 3611L → M: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi370 – 3701V → I: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi383 – 3831A → V: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi391 – 3911N → S: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication
    Mutagenesisi404 – 4041H → K: Strongly increases simvastatin synthase activity upon overexpression in E.coli and abolishes activity with LovD-bound alpha-methylbutyrate; 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 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 413413Acyltransferase LovDPRO_0000430100Add
    BLAST

    Interactioni

    Subunit structurei

    Interacts with LovF.2 Publications

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00000719.

    Structurei

    Secondary structure

    1
    413
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107Combined sources
    Helixi13 – 2614Combined sources
    Beta strandi31 – 399Combined sources
    Beta strandi45 – 539Combined sources
    Helixi75 – 773Combined sources
    Helixi78 – 9114Combined sources
    Helixi101 – 1033Combined sources
    Helixi106 – 1094Combined sources
    Beta strandi113 – 1175Combined sources
    Beta strandi123 – 1264Combined sources
    Helixi134 – 1385Combined sources
    Turni147 – 1493Combined sources
    Helixi151 – 1599Combined sources
    Turni160 – 1645Combined sources
    Beta strandi165 – 1673Combined sources
    Beta strandi173 – 1764Combined sources
    Beta strandi178 – 1803Combined sources
    Turni182 – 1843Combined sources
    Helixi191 – 20313Combined sources
    Helixi207 – 2148Combined sources
    Helixi217 – 2193Combined sources
    Beta strandi223 – 2264Combined sources
    Helixi228 – 2303Combined sources
    Helixi232 – 2376Combined sources
    Beta strandi241 – 2444Combined sources
    Turni246 – 2483Combined sources
    Beta strandi251 – 2544Combined sources
    Helixi257 – 2593Combined sources
    Turni268 – 2703Combined sources
    Helixi276 – 28813Combined sources
    Beta strandi291 – 2944Combined sources
    Helixi296 – 3027Combined sources
    Helixi309 – 32012Combined sources
    Turni323 – 3253Combined sources
    Turni327 – 3304Combined sources
    Beta strandi337 – 3393Combined sources
    Beta strandi341 – 3488Combined sources
    Helixi352 – 3543Combined sources
    Beta strandi361 – 3655Combined sources
    Turni366 – 3683Combined sources
    Beta strandi369 – 3746Combined sources
    Turni375 – 3784Combined sources
    Beta strandi379 – 3846Combined sources
    Beta strandi387 – 3915Combined sources
    Helixi393 – 41220Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliQ9Y7D1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y7D1.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG410JB31. Eukaryota.
    COG1680. LUCA.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.

    Sequencei

    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
    Checksum:i731A140B6E609A24
    GO

    Sequence databases

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

    Genome annotation databases

    KEGGiag:AAD34555.

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliQ9Y7D1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00000719.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAD34555.

    Phylogenomic databases

    eggNOGiENOG410JB31. Eukaryota.
    COG1680. LUCA.

    Enzyme and pathway databases

    UniPathwayiUPA00875.

    Miscellaneous databases

    EvolutionaryTraceiQ9Y7D1.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis."
      Kennedy J., Auclair K., Kendrew S.G., Park C., Vederas J.C., Hutchinson C.R.
      Science 284:1368-1372(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, SUBUNIT.
      Strain: ATCC 20542 / MF4845.
    2. "Biosynthesis of lovastatin analogs with a broadly specific acyltransferase."
      Xie X., Watanabe K., Wojcicki W.A., Wang C.C., Tang Y.
      Chem. Biol. 13:1161-1169(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-76, ACTIVE SITE, BIOTECHNOLOGY.
      Strain: ATCC 20542 / MF4845.
    3. "Rational improvement of simvastatin synthase solubility in Escherichia coli leads to higher whole-cell biocatalytic activity."
      Xie X., Pashkov I., Gao X., Guerrero J.L., Yeates T.O., Tang Y.
      Biotechnol. Bioeng. 102:20-28(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-40 AND CYS-60.
      Strain: ATCC 20542 / MF4845.
    4. "Acyltransferase mediated polyketide release from a fungal megasynthase."
      Xie X., Meehan M.J., Xu W., Dorrestein P.C., Tang Y.
      J. Am. Chem. Soc. 131:8388-8389(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH LOVF.
      Strain: ATCC 20542 / MF4845.
    5. "Directed evolution and structural characterization of a simvastatin synthase."
      Gao X., Xie X., Pashkov I., Sawaya M.R., Laidman J., Zhang W., Cacho R., Yeates T.O., Tang Y.
      Chem. Biol. 16:1064-1074(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH MONACOLIN J; LOVASTATIN AND SIMVASTATIN, BIOTECHNOLOGY, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-12; LYS-26; ALA-86; HIS-161; ALA-190; GLY-275 AND VAL-334, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 20542 / MF4845.
    6. "The role of distant mutations and allosteric regulation on LovD active site dynamics."
      Jimenez-Oses G., Osuna S., Gao X., Sawaya M.R., Gilson L., Collier S.J., Huisman G.W., Yeates T.O., Tang Y., Houk K.N.
      Nat. Chem. Biol. 10:431-436(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), FUNCTION, BIOTECHNOLOGY, PATHWAY, MUTAGENESIS OF ILE-4; ALA-9; LYS-26; ARG-28; ILE-35; ASN-43; ASP-96; SER-109; ALA-123; MET-157; SER-164; SER-172; LEU-174; ALA-178; ASN-191; LEU-192; GLN-241; ALA-247; ARG-250; SER-256; ALA-261; GLY-275; GLN-297; TRP-355; LEU-361; VAL-370; ALA-383; ASN-391 AND HIS-404.
      Strain: ATCC 20542 / MF4845.

    Entry informationi

    Entry nameiLOVD_ASPTE
    AccessioniPrimary (citable) accession number: Q9Y7D1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 3, 2014
    Last sequence update: November 1, 1999
    Last modified: July 6, 2016
    This is version 55 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.