ID   AZIB1_STREG             Reviewed;         401 AA.
AC   B4XY99;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=5-methyl-1-naphthoate 3-hydroxylase {ECO:0000305};
DE            EC=1.14.13.189 {ECO:0000269|PubMed:20485749};
DE   AltName: Full=Azinomycin biosynthesis protein B1 {ECO:0000305};
GN   Name=aziB1 {ECO:0000303|PubMed:18635006};
GN   Synonyms=azi6 {ECO:0000312|EMBL:ABY83145.1};
OS   Streptomyces sahachiroi.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=285525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 33158 / NBRC 13928 / NRRL 2485;
RX   PubMed=18635006; DOI=10.1016/j.chembiol.2008.05.021;
RA   Zhao Q., He Q., Ding W., Tang M., Kang Q., Yu Y., Deng W., Zhang Q.,
RA   Fang J., Tang G., Liu W.;
RT   "Characterization of the azinomycin B biosynthetic gene cluster revealing a
RT   different iterative type I polyketide synthase for naphthoate
RT   biosynthesis.";
RL   Chem. Biol. 15:693-705(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 33158 / NBRC 13928 / NRRL 2485;
RX   PubMed=20485749; DOI=10.1039/b926358f;
RA   Ding W., Deng W., Tang M., Zhang Q., Tang G., Bi Y., Liu W.;
RT   "Biosynthesis of 3-methoxy-5-methyl naphthoic acid and its incorporation
RT   into the antitumor antibiotic azinomycin B.";
RL   Mol. Biosyst. 6:1071-1081(2010).
CC   -!- FUNCTION: Hydroxylase that catalyzes the C3 regiospecific hydroxylation
CC       on the 5-methyl-1-naphthoate to 3-hydroxy-5-methyl-1-naphthoate in the
CC       biosynthesis of the antitumor antibiotic azinomycin B.
CC       {ECO:0000269|PubMed:20485749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methyl-1-naphthoate + H(+) + NADPH + O2 = 3-hydroxy-5-
CC         methyl-1-naphthoate + H2O + NADP(+); Xref=Rhea:RHEA:41452,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78251,
CC         ChEBI:CHEBI:78252; EC=1.14.13.189;
CC         Evidence={ECO:0000269|PubMed:20485749};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q00441};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.4 uM for 5-methyl-1-naphthoate {ECO:0000269|PubMed:20485749};
CC         Note=kcat is 0.8 min(-1). {ECO:0000269|PubMed:20485749};
CC       pH dependence:
CC         Optimum pH is 9.0. {ECO:0000269|PubMed:20485749};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000303|PubMed:18635006}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; EU240558; ABY83145.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4XY99; -.
DR   SMR; B4XY99; -.
DR   KEGG; ag:ABY83145; -.
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; IDA:UniProtKB.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
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; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..401
FT                   /note="5-methyl-1-naphthoate 3-hydroxylase"
FT                   /id="PRO_0000430811"
FT   BINDING         347
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   401 AA;  45109 MW;  70CCE105C5644F40 CRC64;
     MTTEAADATD RLVTAFDHHD PGYTPRTAER INTEIRERGV TWSPAYGGIW ILSRYADVRA
     ALTDWRTYSS ARGVHFPRAE GMPMFSPIDY DPPAQRGIRE RMAAPMTGDA VSAMVPELRR
     MVARLLAPLA GRGHGDLMAE FAEPFAIEVL GVAFGLSESC RARIREATRT MWTYISADRD
     ASKFWPAFHA LLAEEVERVR DEPDGSYLAR LAAMRRDGSP LPDEELYSII VSFCVAGHDN
     TMNSITRLVH TLAQDPALQL RLRREPELRP AVAEEALRRW CPTDRFTRVT TREVTVAGTV
     IPAGARVVLL FDAANRDPEK FPDPDTFDPD RGNSHQHLSF GHGIHHCMGV HLARAEFAAV
     LDELSRLPLF DLEQPSDLHF ENGRHIMFDR VSVRFRTGEE H