BTRV_NIACI
ID BTRV_NIACI Reviewed; 82 AA.
AC Q4H4E3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 21.
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 V;
GN Name=btrV;
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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
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: NAD(P)H:FMN oxidoreductase component of a two-component
CC system involved in the biosynthesis of the side chain of the
CC aminoglycoside antibiotics in the biosynthetic pathway of butirosin.
CC Together with BtrO, mediates hydroxylation of gamma-L-Glu-GABA-S-BtrI.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.86 uM for NADH in the presence of FMN
CC {ECO:0000269|PubMed:15975512};
CC KM=7.25 uM for NADH in the presence of FAD
CC {ECO:0000269|PubMed:15975512};
CC Note=kcat is 1243.13 min(-1) with NADH as substrate in the presence
CC of FMN. kcat is 887.48 min(-1) with NADH as substrate in the presence
CC of FAD.;
CC -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC {ECO:0000269|PubMed:15975512}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15975512}.
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DR EMBL; AB097196; BAE07078.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4H4E3; -.
DR SMR; Q4H4E3; -.
DR PRIDE; Q4H4E3; -.
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 GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR046135; DUF6137.
DR Pfam; PF19634; DUF6137; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..82
FT /note="4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier
FT protein] monooxygenase BtrO"
FT /id="PRO_0000421728"
SQ SEQUENCE 82 AA; 9416 MW; 6456EA01819A7269 CRC64;
MDNKERNTLY QVVYAISGVT GEDGDELVET FKQGPMEVDK RDFFEIVQRV ESLFDCTLDM
NLEGPYLIHA DEIVTKITKL NV
