ID   COTB4_STRMJ             Reviewed;         459 AA.
AC   C9K1X7;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Cyclooctatin synthase {ECO:0000305};
DE            EC=1.14.99.62 {ECO:0000269|PubMed:19635410, ECO:0000269|PubMed:27216162};
GN   Name=cotB4 {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 hydroxylation of
CC       cyclooctat-9-ene-5,7-diol at C-18 to yield the final product,
CC       cyclooctatin. {ECO:0000269|PubMed:19635410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + cyclooctat-9-ene-5,7-diol + O2 = A + cyclooctatin + H2O;
CC         Xref=Rhea:RHEA:56824, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:78370,
CC         ChEBI:CHEBI:141020; EC=1.14.99.62;
CC         Evidence={ECO:0000269|PubMed:19635410, ECO:0000269|PubMed:27216162};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56825;
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.
CC       {ECO:0000255|RuleBase:RU000461}.
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DR   EMBL; AB448947; BAI44340.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9K1X7; -.
DR   SMR; C9K1X7; -.
DR   KEGG; ag:BAI44340; -.
DR   BioCyc; MetaCyc:MON-18588; -.
DR   BRENDA; 1.14.99.62; 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; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
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="Cyclooctatin synthase"
FT                   /id="PRO_0000452044"
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;  50903 MW;  E82AFEE3E68FDC61 CRC64;
     MKDFFRMRTA QQPATRHWRH TVAPGGLPLA GHALLMARKP LQFLASLPAH GDLVELRLGP
     RPVYLPCHPE LVQQVLVNAR VYDTGGPVKE KAKPILGNGL ITSDWADHRR QRRLVQPAFH
     TARIAKYAEV MERECEAEST AWTARRPIDV SHEMLALTAR VTARALFSTD MAPHAVAEIQ
     HCLPIVVEGA YRQAIDPTGL LAKLPLAANR RFDDALARLN QLIDRMIDDY KASDDGDRGD
     VLSALFAAQD DETGGTMSDQ EIHDQVMTLL LAGIETTASA LTWAWFLLGR NPGAEAALHA
     EVDEVLGGRA PRYADVPRLA YTQRVFSEAL RLFPPAWLFT RTTTETTELG GRRLPPASDV
     LISPYVLHRD PALFPRPDSF DPDRWLPERA KEVTRGSYLP FGGGSRKCIG DVFGMTEATL
     ALAAIAGRWR MRPIPGTKIR PRPQMSLTAG PLRMIPEPR