ID   BTRM_NIACI              Reviewed;         389 AA.
AC   Q4H4F8;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=2-deoxystreptamine N-acetyl-D-glucosaminyltransferase;
DE            EC=2.4.1.283;
DE   AltName: Full=Butirosin biosynthesis protein M;
GN   Name=btrM;
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, AND PATHWAY.
RX   PubMed=15701005; DOI=10.1021/ja044921b;
RA   Kudo F., Kawabe K., Kuriki H., Eguchi T., Kakinuma K.;
RT   "A new family of glucose-1-phosphate/glucosamine-1-phosphate
RT   nucleotidylyltransferase in the biosynthetic pathways for antibiotics.";
RL   J. Am. Chem. Soc. 127:1711-1718(2005).
CC   -!- FUNCTION: Glycosyltransferase involved in the biosynthesis of butirosin
CC       by mediating conversion of 2-deoxystreptamine (2-DOS) to 2'-N-
CC       acetylparomamine using UDP-alpha-D-glucosamine as sugar donor.
CC       {ECO:0000305|PubMed:15701005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxystreptamine + UDP-N-acetyl-alpha-D-glucosamine = 2'-N-
CC         acetylparomamine + H(+) + UDP; Xref=Rhea:RHEA:33947,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:65010, ChEBI:CHEBI:65069; EC=2.4.1.283;
CC   -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC       {ECO:0000269|PubMed:15701005}.
CC   -!- MISCELLANEOUS: In contrast to KanF enzyme in S.kanamyceticus, can only
CC       accept UDP-N-acetyl-alpha-D-glucosamine and not UDP-alpha-D-glucose.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AB097196; BAE07063.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H4F8; -.
DR   SMR; Q4H4F8; -.
DR   KEGG; ag:BAE07063; -.
DR   BioCyc; MetaCyc:MON-17233; -.
DR   UniPathway; UPA00964; -.
DR   GO; GO:0102319; F:2-deoxystreptamine N-acetyl-D-glucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..389
FT                   /note="2-deoxystreptamine N-acetyl-D-
FT                   glucosaminyltransferase"
FT                   /id="PRO_0000421741"
SQ   SEQUENCE   389 AA;  43387 MW;  B2124449461E0FFD CRC64;
     MGGMQVQITN LTEWLADQGV RQDVLTTGIP GIPRTLQLRD RLTVHSVRFM TLPFKSSQTG
     TVFLDQSWFM GAVKWIVLNG KKNNYDAIHV HASGVVWPLL AGMFAQKYLK KPLILTIHCS
     RIFTYKPMNK WDQFVHDFVK SVELKSIKLS HKAVVLTDKR LDSYNRLLED SSKMTAISDC
     IGSNHLSHSI DCPFCSRLKT ELLGKKTVLF LGRIAHEKGW STFVSVAKEL ADKIGDLQFI
     VCGDGPQREA MEEQIKAANL QNQFRITGFI SHKFVSCYLH HAQLFLLPSH HEEFGGSLIE
     AAIAGVPIIS TNNGGPADIF THGETAILKD PGDVSGIADE AYKILTNDSV AESLRLHSRP
     EVVSKFLPHC VYPNYLNLYS SKEAAVHEG