TPC1_STRAW
ID TPC1_STRAW Reviewed; 335 AA.
AC Q82RR7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Avermitilol synthase;
DE EC=4.2.3.96;
GN Name=tpc1; OrderedLocusNames=SAV_76;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20536237; DOI=10.1021/ja103087w;
RA Chou W.K., Fanizza I., Uchiyama T., Komatsu M., Ikeda H., Cane D.E.;
RT "Genome mining in Streptomyces avermitilis: cloning and characterization of
RT SAV_76, the synthase for a new sesquiterpene, avermitilol.";
RL J. Am. Chem. Soc. 132:8850-8851(2010).
CC -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate to
CC avermitilol. {ECO:0000269|PubMed:20536237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = avermitilol +
CC diphosphate; Xref=Rhea:RHEA:32023, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63702, ChEBI:CHEBI:175763;
CC EC=4.2.3.96; Evidence={ECO:0000269|PubMed:20536237};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.06 uM for farnesyl diphosphate {ECO:0000269|PubMed:20536237};
CC Note=kcat is 0.04 sec(-1).;
CC -!- MISCELLANEOUS: The recombinent enzyme produces avermitilol (85%),
CC accompanied by small quantities of germacrene A, germacrene B and
CC viridiflorol. {ECO:0000305|PubMed:20536237}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; BA000030; BAC67785.1; -; Genomic_DNA.
DR RefSeq; WP_010981512.1; NZ_JZJK01000037.1.
DR AlphaFoldDB; Q82RR7; -.
DR SMR; Q82RR7; -.
DR STRING; 227882.SAV_76; -.
DR EnsemblBacteria; BAC67785; BAC67785; SAVERM_76.
DR KEGG; sma:SAVERM_76; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_042538_4_0_11; -.
DR OMA; EWLLSMA; -.
DR OrthoDB; 1869158at2; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..335
FT /note="Avermitilol synthase"
FT /id="PRO_0000418451"
FT MOTIF 80..84
FT /note="DDXXD motif"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 36480 MW; 49B8477E2D52666F CRC64;
MPQDIDFGLP APAGISPGLE ATRRHNLGWV RRLGLVGDGP SLAWYTSWDM PRLAACGFPH
ARGAALDLCA DAMAFFFVFD DQFDGPLGRD PARAARVCRR LTGIVHGAGP GPGADACSAA
FADVWARSTD GAHPGWVART AHEWEYYFAA QAHEAINRLR GTPGDMESYL QVRRGIAGTD
LPLSLGERAA GITVPAAAFH SPQLRIMREA AIDVTLMCND VYSLEKEEAR GDMDNLVLVI
EHARRCTRDE AVTAARGEVA RRVIRFEQLA REVPALCAQL GLSAVERAHV DTYLGVMEAW
MSGYHAWQTQ TRRYTGAPHV LPSTGPGYFD EVLPT
