ID   BTRG_NIACI              Reviewed;         156 AA.
AC   Q4H4F0;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Gamma-L-glutamyl-butirosin B gamma-glutamyl cyclotransferase;
DE            EC=4.3.2.6;
DE   AltName: Full=Butirosin biosynthesis protein G;
GN   Name=btrG;
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=17462573; DOI=10.1016/j.chembiol.2007.02.005;
RA   Llewellyn N.M., Li Y., Spencer J.B.;
RT   "Biosynthesis of butirosin: transfer and deprotection of the unique amino
RT   acid side chain.";
RL   Chem. Biol. 14:379-386(2007).
CC   -!- FUNCTION: Cyclotransferase that catalyzes the last step in the
CC       biosynthesis of the aminoglycoside antibiotic butirosin B. Cleaves the
CC       amide bond via transamidation using the alpha-amine of the terminal
CC       gamma-L-glutamate of the side chain, releasing it as the cyclic 5-
CC       oxoproline. {ECO:0000269|PubMed:17462573}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamyl-butirosin B = 5-oxo-L-proline + butirosin B;
CC         Xref=Rhea:RHEA:33995, ChEBI:CHEBI:58402, ChEBI:CHEBI:65085,
CC         ChEBI:CHEBI:65086; EC=4.3.2.6;
CC         Evidence={ECO:0000269|PubMed:17462573};
CC   -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC       {ECO:0000269|PubMed:17462573}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB097196; BAE07071.1; -; Genomic_DNA.
DR   EMBL; AJ781030; CAG77425.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H4F0; -.
DR   SMR; Q4H4F0; -.
DR   KEGG; ag:BAE07071; -.
DR   BioCyc; MetaCyc:MON-17276; -.
DR   UniPathway; UPA00964; -.
DR   GO; GO:0016842; F:amidine-lyase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   CDD; cd06661; GGCT_like; 1.
DR   InterPro; IPR009288; AIG2-like_dom.
DR   InterPro; IPR013024; GGCT-like.
DR   InterPro; IPR036568; GGCT-like_sf.
DR   Pfam; PF06094; GGACT; 1.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Lyase.
FT   CHAIN           1..156
FT                   /note="Gamma-L-glutamyl-butirosin B gamma-glutamyl
FT                   cyclotransferase"
FT                   /id="PRO_0000421758"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         24..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   156 AA;  18061 MW;  CDE13F1EBDF233CA CRC64;
     MISWTKAFTK PLKGRIFMPN LFVYGTLREG ENNHKYMKEA TLLSRKASIA GSLVDTGNGY
     PGLLLENQLV AGEWYEVSEE TLKRIDELEE YFGPGDTRNL FDRIECQVNE SGGTHLGWTY
     VYNRDDYLET RFSDWKQYRL QHASGIEEKQ DVPHSL