ID   NOVI_STRNV              Reviewed;         407 AA.
AC   Q9L9F9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Cytochrome P450 NovI;
DE            EC=1.14.-.-;
DE   AltName: Full=Novobiocin biosynthesis protein I;
GN   Name=novI;
OS   Streptomyces niveus (Streptomyces spheroides).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=193462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA   Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT   "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT   spheroides NCIB 11891.";
RL   Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=11325587; DOI=10.1016/s1074-5521(01)00009-6;
RA   Chen H., Walsh C.T.;
RT   "Coumarin formation in novobiocin biosynthesis: beta-hydroxylation of the
RT   aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI.";
RL   Chem. Biol. 8:301-312(2001).
CC   -!- FUNCTION: Together with NovH, involved in the formation of a beta-OH-
CC       Tyr intermediate in the novobiocin biosynthesis pathway, an
CC       aminocoumarin family antibiotic that targets bacterial DNA gyrases.
CC       Acts as a cytochrome P450-type monooxygenase with specificity for the
CC       tyrosyl-S-NovH acyl enzyme (L-Tyr-S-NovH) to form the beta-OH-Tyr
CC       intermediate (L-beta-OH-Tyr-S-NovH). {ECO:0000269|PubMed:11325587}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC       {ECO:0000269|PubMed:11325587}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF170880; AAF67502.1; -; Genomic_DNA.
DR   RefSeq; WP_069626139.1; NZ_MDCR01000039.1.
DR   AlphaFoldDB; Q9L9F9; -.
DR   SMR; Q9L9F9; -.
DR   KEGG; ag:AAF67502; -.
DR   BioCyc; MetaCyc:MON-18085; -.
DR   UniPathway; UPA01035; -.
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:0043642; P:novobiocin biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..407
FT                   /note="Cytochrome P450 NovI"
FT                   /id="PRO_0000423999"
FT   BINDING         357
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"
SQ   SEQUENCE   407 AA;  45176 MW;  7A8105A95ED9E7A9 CRC64;
     MSTRPTVSPS ELEQIDLASP VLHAEYELDE IFRHLRADEP VYWQQPRNEQ PGFWVISRHA
     DVNEVYKDKE HFTTEHGNAL ATLLTGGDSA SGAMLAVTDG VRHHQVRNVL SRGFSARMLD
     LIAHTLQETV DGLLLAALER GECDAAQDIA ADVPLGAICD LLEIPHADRK YLLGLTSHAW
     STDYADEPPE ESWVAKNEIL LYFSKLLKER RGGVREDMVS LLANCRIDGD PLKAAEQMAN
     CYGLMIGGDE TGRHAITGTI LALIQNPDQW RALKNGDVDL NTATEEALRW TVPSLHGGRK
     ATGDVVINGR RINAGDVVSV WISSANRDET VFDAPDEFNL ARTPNKHFTF AYGSHYCLGH
     YLGRMEVYAV LDGLRRLVGD LEQIGEERWI YSSILHGMSS LPIRITG