(data stored in ACNUC7421 zone)

SWISSPROT: 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   08-MAY-2019, entry version 92.
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 /
OS   NBRC 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 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   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 /
RC   NRRL 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
RT   characterization of SAV_76, the synthase for a new sesquiterpene,
RT   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
CC         {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}.
DR   EMBL; BA000030; BAC67785.1; -; Genomic_DNA.
DR   RefSeq; WP_010981512.1; NZ_JZJK01000037.1.
DR   SMR; Q82RR7; -.
DR   STRING; 227882.SAV_76; -.
DR   EnsemblBacteria; BAC67785; BAC67785; SAVERM_76.
DR   KEGG; sma:SAVERM_76; -.
DR   eggNOG; ENOG4108X7A; Bacteria.
DR   eggNOG; ENOG410XSNU; LUCA.
DR   HOGENOM; HOG000146717; -.
DR   KO; K18110; -.
DR   OMA; LCFGLFE; -.
DR   OrthoDB; 1869158at2; -.
DR   BioCyc; SAVE227882:G1G23-86-MONOMER; -.
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;
DR   PRODOM; Q82RR7.
DR   SWISS-2DPAGE; Q82RR7.
KW   Complete proteome; Lyase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    335       Avermitilol synthase.
FT                                /FTId=PRO_0000418451.
FT   MOTIF        80     84       DDXXD motif.
FT   METAL        80     80       Magnesium 1. {ECO:0000250}.
FT   METAL        80     80       Magnesium 2. {ECO:0000250}.
FT   METAL        84     84       Magnesium 1. {ECO:0000250}.
FT   METAL        84     84       Magnesium 2. {ECO:0000250}.
FT   METAL       219    219       Magnesium 3. {ECO:0000250}.
FT   METAL       223    223       Magnesium 3. {ECO:0000250}.
FT   METAL       227    227       Magnesium 3. {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
//

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