ID   OTCC_STRRM              Reviewed;         503 AA.
AC   Q58PK7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Anhydrotetracycline monooxygenase {ECO:0000305};
DE            EC=1.14.13.38 {ECO:0000269|PubMed:16148009};
GN   Name=otcC {ECO:0000303|PubMed:16148009};
OS   Streptomyces rimosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-9; GLY-11 AND GLY-14.
RC   STRAIN=R6-500;
RX   PubMed=16148009; DOI=10.1074/jbc.m503191200;
RA   Peric-Concha N., Borovicka B., Long P.F., Hranueli D., Waterman P.G.,
RA   Hunter I.S.;
RT   "Ablation of the otcC gene encoding a post-polyketide hydroxylase from the
RT   oxytetracyline biosynthetic pathway in Streptomyces rimosus results in
RT   novel polyketides with altered chain length.";
RL   J. Biol. Chem. 280:37455-37460(2005).
CC   -!- FUNCTION: Catalyzes hydroxylation of the anthracycline structure at
CC       position C-6 during the biosynthesis of oxytetracyline.
CC       {ECO:0000269|PubMed:16148009}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=anhydrotetracycline + H(+) + NADPH + O2 = 5a,11a-
CC         dehydrotetracycline + H2O + NADP(+); Xref=Rhea:RHEA:11976,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58032,
CC         ChEBI:CHEBI:58349; EC=1.14.13.38;
CC         Evidence={ECO:0000269|PubMed:16148009};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q54530};
CC   -!- PATHWAY: Antibiotic biosynthesis; oxytetracycline biosynthesis.
CC       {ECO:0000269|PubMed:16148009}.
CC   -!- DISRUPTION PHENOTYPE: Mutants fail to produce oxytetracyline but
CC       instead synthesize novel polyketides of shorter chain length.
CC       {ECO:0000269|PubMed:16148009}.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AY916128; AAX48941.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q58PK7; -.
DR   SMR; Q58PK7; -.
DR   BRENDA; 1.14.13.38; 6084.
DR   UniPathway; UPA00926; -.
DR   GO; GO:0047670; F:anhydrotetracycline monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; FAD; Flavoprotein; NADP; Oxidoreductase.
FT   CHAIN           1..503
FT                   /note="Anhydrotetracycline monooxygenase"
FT                   /id="PRO_0000430628"
FT   MUTAGEN         9
FT                   /note="G->A: Lack of activity; when associated with A-11
FT                   and A-14."
FT                   /evidence="ECO:0000269|PubMed:16148009"
FT   MUTAGEN         11
FT                   /note="G->A: Lack of activity; when associated with A-9 and
FT                   A-14."
FT                   /evidence="ECO:0000269|PubMed:16148009"
FT   MUTAGEN         14
FT                   /note="G->A: Lack of activity; when associated with A-9 and
FT                   A-11."
FT                   /evidence="ECO:0000269|PubMed:16148009"
SQ   SEQUENCE   503 AA;  54565 MW;  80ABD5948FE25894 CRC64;
     MRYDVVIAGA GPTGLMLACE LRLAGARTLV LERLAERVDF SKALGVHART VELLDMRGLG
     RGFQAEAPKL RGGNFASLGV PLDFSSFDTR HPYALFVPQV RTETLLTGRA LELGAELRRG
     HAVTALEQDA DGVTVSVTGP EGPYEVECAY LVGCDGGGIT VRKLLGIDFP GQDPHMFAVI
     ADARFREELP HGEGMGPMRP YGVMRHDLRA WFAAFPLEPD VYRATVAFFD RPYADRRAPV
     TEEDVRAALT EVAGSDFGMH DVRWLSRLTD TSRQAERYRD GRVLLAGDAC HIHLPAGGQG
     LNLGFQDAVN LGWKLGATIA GTAPPELLDT YEAERRPIAA GVLRNTRAQA VLIDPDPRYE
     GLRELMIELL HVPETNRYLA GLISALDVRY PMAGEHPLLG RRVPDLPLVT EDGTRQLSTY
     FHAARGVLLT LGCDQPLADE AAAWKDRVDL VAAEGVADPG SAVDGLTALL VRPDGYICWT
     AAPETGTDGL TDALRTWFGP PAM