ID   COTB3_STRMJ             Reviewed;         459 AA.
AC   C9K1X6;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Cyclooctat-9-en-7-ol 5-monooxygenase {ECO:0000305};
DE            EC=1.14.99.61 {ECO:0000269|PubMed:19635410, ECO:0000269|PubMed:27216162};
GN   Name=cotB3 {ECO:0000303|PubMed:19635410};
OS   Streptomyces melanosporofaciens.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=67327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=MI614-43F2;
RX   PubMed=19635410; DOI=10.1016/j.chembiol.2009.06.007;
RA   Kim S.Y., Zhao P., Igarashi M., Sawa R., Tomita T., Nishiyama M.,
RA   Kuzuyama T.;
RT   "Cloning and heterologous expression of the cyclooctatin biosynthetic gene
RT   cluster afford a diterpene cyclase and two p450 hydroxylases.";
RL   Chem. Biol. 16:736-743(2009).
RN   [2]
RP   CATALYTIC ACTIVITY.
RX   PubMed=27216162; DOI=10.1186/s12934-016-0487-6;
RA   Goerner C., Schrepfer P., Redai V., Wallrapp F., Loll B., Eisenreich W.,
RA   Haslbeck M., Brueck T.;
RT   "Identification, characterization and molecular adaptation of class I redox
RT   systems for the production of hydroxylated diterpenoids.";
RL   Microb. Cell Fact. 15:86-86(2016).
CC   -!- FUNCTION: Involved in the biosynthesis of cyclooctatin, a potent
CC       inhibitor of lysophospholipase. Catalyzes the stereospecific
CC       hydroxylation of cyclooctat-9-en-7-ol to form cyclooctat-9-ene-5,7-
CC       diol. {ECO:0000269|PubMed:19635410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + cyclooctat-9-en-7-ol + O2 = A + cyclooctat-9-ene-5,7-
CC         diol + H2O; Xref=Rhea:RHEA:56820, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:78352, ChEBI:CHEBI:141020; EC=1.14.99.61;
CC         Evidence={ECO:0000269|PubMed:19635410, ECO:0000269|PubMed:27216162};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56821;
CC         Evidence={ECO:0000269|PubMed:19635410, ECO:0000269|PubMed:27216162};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q9K498};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB448947; BAI44339.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9K1X6; -.
DR   SMR; C9K1X6; -.
DR   KEGG; ag:BAI44339; -.
DR   BioCyc; MetaCyc:MON-18587; -.
DR   BRENDA; 1.14.99.61; 13958.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..459
FT                   /note="Cyclooctat-9-en-7-ol 5-monooxygenase"
FT                   /id="PRO_0000452043"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         408
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:Q9K498"
SQ   SEQUENCE   459 AA;  50687 MW;  84B6DB0E52119333 CRC64;
     MRERGPVTPA KSSAPPERPW TTGTAPGSVP LLGHTMALWR RPLQFLASLP AHGDLVEVRL
     GPSRAYLACH PELVRQVLLN PRVFDKGGVF DKARQLLGNS LSVSRGEDHR YQRRMIQPAF
     HTPKIAAYTA AVADDTRAAI GSWEPGRTLD ISDTMHALLM RVAARTLFST GIDEATIDEA
     RHCLRIVSDG IYKRTMAPLG IMEKLPTPGN RRYDRANARL RQIVDEMIRE RRRSGADHGD
     LLSTLLRAEH PETGKGLDDG EVLDQVVTFL VAGSETTAST LAFVFHLLGA HPEVEKRVHA
     EIDEILEGRS PTFEDLPSLE YTRGVITESL RLYPPSWMAM RVTAAETELG GRTVPAGTMI
     LYSAQALHHN PELFPDPERF DPERWLGDRA KEVERGALLP FGAGSHKCIG DVLALTETAL
     IVATIASRWR LRPVPGTTLR PEPKATLEPG PLPMVCEPR