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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)DescriptionActionsGraphical viewLength
    Binding sitei73Monacolin J1
    Active sitei76Acyl-ester intermediate2 Publications1
    Binding sitei173Monacolin J1
    Binding sitei188Monacolin J1
    Binding sitei258Monacolin J1
    Binding sitei3662-methylbutyrate; via amide nitrogen1
    Binding sitei388Monacolin J1
    Binding sitei390Monacolin J1

    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

    BioCyciMetaCyc:MONOMER-18785.
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi4I → 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 Publication1
    Mutagenesisi9A → 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 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-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 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-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 Publication1
    Mutagenesisi35I → 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 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-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 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-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 Publication1
    Mutagenesisi109S → 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 Publication1
    Mutagenesisi123A → 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 Publication1
    Mutagenesisi157M → 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 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-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 Publication1
    Mutagenesisi172S → 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 Publication1
    Mutagenesisi174L → 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 Publication1
    Mutagenesisi178A → 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 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-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 Publication1
    Mutagenesisi192L → 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 Publication1
    Mutagenesisi241Q → 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 Publication1
    Mutagenesisi247A → 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 Publication1
    Mutagenesisi250R → 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 Publication1
    Mutagenesisi256S → 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 Publication1
    Mutagenesisi261A → 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 Publication1
    Mutagenesisi275G → 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 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-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 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-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 Publication1
    Mutagenesisi361L → 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 Publication1
    Mutagenesisi370V → 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 Publication1
    Mutagenesisi383A → 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 Publication1
    Mutagenesisi391N → 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 Publication1
    Mutagenesisi404H → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004301001 – 413Acyltransferase LovDAdd BLAST413

    Interactioni

    Subunit structurei

    Interacts with LovF.2 Publications

    Protein-protein interaction databases

    STRINGi33178.CADATEAP00000719.

    Structurei

    Secondary structure

    1413
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi4 – 10Combined sources7
    Helixi13 – 26Combined sources14
    Beta strandi31 – 39Combined sources9
    Beta strandi45 – 53Combined sources9
    Helixi75 – 77Combined sources3
    Helixi78 – 91Combined sources14
    Helixi101 – 103Combined sources3
    Helixi106 – 109Combined sources4
    Beta strandi113 – 117Combined sources5
    Beta strandi123 – 126Combined sources4
    Helixi134 – 138Combined sources5
    Turni147 – 149Combined sources3
    Helixi151 – 159Combined sources9
    Turni160 – 164Combined sources5
    Beta strandi165 – 167Combined sources3
    Beta strandi173 – 176Combined sources4
    Beta strandi178 – 180Combined sources3
    Turni182 – 184Combined sources3
    Helixi191 – 203Combined sources13
    Helixi207 – 214Combined sources8
    Helixi217 – 219Combined sources3
    Beta strandi223 – 226Combined sources4
    Helixi228 – 230Combined sources3
    Helixi232 – 237Combined sources6
    Beta strandi241 – 244Combined sources4
    Turni246 – 248Combined sources3
    Beta strandi251 – 254Combined sources4
    Helixi257 – 259Combined sources3
    Turni268 – 270Combined sources3
    Helixi276 – 288Combined sources13
    Beta strandi291 – 294Combined sources4
    Helixi296 – 302Combined sources7
    Helixi309 – 320Combined sources12
    Turni323 – 325Combined sources3
    Turni327 – 330Combined sources4
    Beta strandi337 – 339Combined sources3
    Beta strandi341 – 348Combined sources8
    Helixi352 – 354Combined sources3
    Beta strandi361 – 365Combined sources5
    Turni366 – 368Combined sources3
    Beta strandi369 – 374Combined sources6
    Turni375 – 378Combined sources4
    Beta strandi379 – 384Combined sources6
    Beta strandi387 – 391Combined sources5
    Helixi393 – 412Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliQ9Y7D1.
    SMRiQ9Y7D1.
    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
    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[»]
    ProteinModelPortaliQ9Y7D1.
    SMRiQ9Y7D1.
    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.
    BioCyciMetaCyc:MONOMER-18785.

    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...

    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: November 2, 2016
    This is version 56 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.