ID   NCSB3_STRCZ             Reviewed;         410 AA.
AC   Q84HB6;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase {ECO:0000303|PubMed:15797213};
DE            EC=1.14.15.31 {ECO:0000269|PubMed:20735485};
DE   AltName: Full=Neocarzinostatin biosynthesis protein B3 {ECO:0000305};
DE   AltName: Full=P450 hydroxylase {ECO:0000303|PubMed:20735485};
GN   Name=ncsB3 {ECO:0000303|PubMed:15797213};
OS   Streptomyces carzinostaticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1897;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 15944 / E-793 / F-51;
RX   PubMed=15797213; DOI=10.1016/j.chembiol.2004.12.013;
RA   Liu W., Nonaka K., Nie L., Zhang J., Christenson S.D., Bae J.,
RA   Van Lanen S.G., Zazopoulos E., Farnet C.M., Yang C.F., Shen B.;
RT   "The neocarzinostatin biosynthetic gene cluster from Streptomyces
RT   carzinostaticus ATCC 15944 involving two iterative type I polyketide
RT   synthases.";
RL   Chem. Biol. 12:293-302(2005).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20735485; DOI=10.1111/j.1574-6968.2010.02075.x;
RA   Hang V.T., Oh T.J., Yamaguchi T., Sohng J.K.;
RT   "In vivo characterization of NcsB3 to establish the complete biosynthesis
RT   of the naphthoic acid moiety of the neocarzinostatin chromophore.";
RL   FEMS Microbiol. Lett. 311:119-125(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of the naphthoic acid (NA)
CC       moiety in the chromophore of the enedyine antitumor antibiotic
CC       neocarzinostatin (NCS). Catalyzes the hydroxylation at C-7 position of
CC       2-hydroxy-5-methyl-1-naphthoate to yield 2,7-dihydroxy-5-methyl-1-
CC       naphthoate. {ECO:0000269|PubMed:20735485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-5-methyl-1-naphthoate + 2 H(+) + O2 + 2 reduced
CC         [2Fe-2S]-[ferredoxin] = 2,7-dihydroxy-5-methyl-1-naphthoate + H2O + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:42828, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:78281, ChEBI:CHEBI:82757;
CC         EC=1.14.15.31; Evidence={ECO:0000269|PubMed:20735485};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q00441};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:15797213}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY117439; AAM77997.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84HB6; -.
DR   SMR; Q84HB6; -.
DR   KEGG; ag:AAM77997; -.
DR   BRENDA; 1.14.15.31; 13527.
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; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Heme; Iron; Metal-binding; Monooxygenase;
KW   Oxidoreductase.
FT   CHAIN           1..410
FT                   /note="2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase"
FT                   /id="PRO_0000430703"
FT   BINDING         350
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:Q00441"
SQ   SEQUENCE   410 AA;  45493 MW;  4646AB890FDACF42 CRC64;
     MCPYRLDPEG ADTHGETARL REQGPIARVE LQDGVLAWSV HDYAVAKQIM ADERFSKNPR
     KNWPAYINGE ISNGWPLITW VAMDTMATQD GADHARLRKL LLKAFTERRV ESMRPHIEKT
     VKELLDNMAA KADDEIVDIK EMFHAELPTR LMCDLFGVPE ERRAEVLAGG HKNIDTRISS
     EAAEANLGQW QEAISDLVEY KRHHPGDDLT SALIEARDEG SRLSDSELIG TLHLLLGAGS
     ETLVNALAHS SLALLVDADL RKKVTSGEIP WVNVWEETLR VESPVAHLPF RYATEDFEIG
     GVKISKGDPL LVDFAGIGRD PAVHSDAPDE FDALRPDKTH LSFGHGVHYC LGARLAKHAW
     MIGIPALFER FPDMELAVRR DELKGQGSFV VNGHASLPVH LKGRAAALAR