ID   BTRO_NIACI              Reviewed;         341 AA.
AC   Q4H4E5;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase BtrO;
DE            EC=1.14.14.13;
DE   AltName: Full=Butirosin biosynthesis protein O;
GN   Name=btrO;
OS   Niallia circulans (Bacillus circulans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=1397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX   PubMed=16156513; DOI=10.1038/ja.2005.47;
RA   Kudo F., Numakura M., Tamegai H., Yamamoto H., Eguchi T., Kakinuma K.;
RT   "Extended sequence and functional analysis of the butirosin biosynthetic
RT   gene cluster in Bacillus circulans SANK 72073.";
RL   J. Antibiot. 58:373-379(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RA   Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT   deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT   neomycin, lividomycin, paromomycin and butirosin.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX   PubMed=15975512; DOI=10.1016/j.chembiol.2005.04.010;
RA   Li Y., Llewellyn N.M., Giri R., Huang F., Spencer J.B.;
RT   "Biosynthesis of the unique amino acid side chain of butirosin: possible
RT   protective-group chemistry in an acyl carrier protein-mediated pathway.";
RL   Chem. Biol. 12:665-675(2005).
CC   -!- FUNCTION: Monooxygenase component of a two-component system involved in
CC       the biosynthesis of the side chain of the aminoglycoside antibiotics in
CC       the biosynthetic pathway of butirosin. Together with BtrV, mediates
CC       hydroxylation of gamma-L-Glu-GABA-S-BtrI. Not able to hydroxylate free
CC       substrates, activation by the acyl-carrier protein is mandatory.
CC       Octanoyl-S-[BtrI acyl-carrier protein] is also accepted as substrate.
CC       {ECO:0000269|PubMed:15975512}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(gamma-L-glutamylamino)butanoy-[BtrI ACP] + FMNH2 + O2 = 4-
CC         (gamma-L-glutamylamino)-(2S)-2-hydroxybutanoyl-[BtrI ACP] + FMN +
CC         H(+) + H2O; Xref=Rhea:RHEA:53960, Rhea:RHEA-COMP:13743, Rhea:RHEA-
CC         COMP:13745, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:137998,
CC         ChEBI:CHEBI:137999; EC=1.14.14.13;
CC         Evidence={ECO:0000269|PubMed:15975512};
CC   -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC       {ECO:0000269|PubMed:15975512}.
CC   -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AB097196; BAE07076.1; -; Genomic_DNA.
DR   EMBL; AJ781030; CAG77430.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H4E5; -.
DR   SMR; Q4H4E5; -.
DR   KEGG; ag:BAE07076; -.
DR   BioCyc; MetaCyc:MON-17274; -.
DR   BRENDA; 1.14.14.13; 649.
DR   UniPathway; UPA00964; -.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; TAS:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Flavoprotein; FMN; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..341
FT                   /note="4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier
FT                   protein] monooxygenase BtrO"
FT                   /id="PRO_0000421757"
SQ   SEQUENCE   341 AA;  38740 MW;  C01D3A237F9E9E0E CRC64;
     MIALDTIQYY GQIPGVNHYN GKKEFMENAV KIAQLSDAYG IVGSLSFFNH SVLDPWAVSS
     VIMRHTERHV PLIALQPYMY PPYTAAKLIQ SFTYLYDRRI DLNMITGAVT GELQQTGGYI
     DHSSRYKKLH EYVQVLRLLL ESDSAVSFKG DYYELNNLEF KPLLPDKRLF PRIFMSGSSE
     EGLETGLKAA DFVVTHPGPL EHFKRHFSEK VQGSAVQSAI RIEIIARESA EQAWKIAHAR
     YPGNRQGKIQ LRMKTNSESS WQRMLAELAL ASETYDEVFW MGGYMNGGIY SPVLVGDYEQ
     VAAYLNEYYK LGVKAVLLGS MYSEEDFIHF SRVKEGISNP V