BTRL_NIACI
ID BTRL_NIACI Reviewed; 604 AA.
AC Q4H4F7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Neamine phosphoribosyltransferase;
DE EC=2.4.2.49;
DE AltName: Full=Butirosin biosynthesis protein P;
GN Name=btrL;
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, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP PATHWAY.
RC STRAIN=SANK 72073;
RX PubMed=17482823; DOI=10.1016/j.bmc.2007.04.040;
RA Kudo F., Fujii T., Kinoshita S., Eguchi T.;
RT "Unique O-ribosylation in the biosynthesis of butirosin.";
RL Bioorg. Med. Chem. 15:4360-4368(2007).
CC -!- FUNCTION: Catalyzes phosphoribosylation of neamine using 5-
CC phosphoribosyl-1-diphosphate (PRPP) as a phosphoribosyl donor to
CC generate 5''-phosphoribostamycin in the biosynthetic pathway of
CC butirosin. {ECO:0000269|PubMed:17482823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + neamine = 5''-
CC phosphoribostamycin + diphosphate; Xref=Rhea:RHEA:34043,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:65076,
CC ChEBI:CHEBI:65082; EC=2.4.2.49;
CC Evidence={ECO:0000269|PubMed:17482823};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:17482823};
CC Note=Divalent metal ion. {ECO:0000269|PubMed:17482823};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17482823};
CC Temperature dependence:
CC Optimum temperature is 27-32 degrees Celsius.
CC {ECO:0000269|PubMed:17482823};
CC -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC {ECO:0000269|PubMed:17482823}.
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DR EMBL; AB097196; BAE07064.1; -; Genomic_DNA.
DR EMBL; AJ781030; CAG77418.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4H4F7; -.
DR KEGG; ag:BAE07064; -.
DR BioCyc; MetaCyc:MON-17254; -.
DR UniPathway; UPA00964; -.
DR GO; GO:0016763; F:pentosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR029057; PRTase-like.
DR SUPFAM; SSF53271; SSF53271; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT CHAIN 1..604
FT /note="Neamine phosphoribosyltransferase"
FT /id="PRO_0000421727"
SQ SEQUENCE 604 AA; 68618 MW; E848DDB3E02606EC CRC64;
MKDNPISLFH ELESYVRGSK DTLHRYMYAC ILEQRLADLL LLSRCGVHPD DEDRLAVRLA
SQRSLCVQAA SDLAEGTEEA RGSTPAWPDC KVTKSSAAQK RPELLSLVKV MQELRTPECS
GYDLCDLEVC REDALHWLRD HADPSSPPVL IGVRTGGAFY APLWSSALQQ RWGNKALYHT
VRALRMPSDP GASLYLPEEL SILPAAIEPD TDIVILEDQP HTGGTVLELA GRLSAKYRLN
KPVWVSSPGR LFQIENGRLA KCSDRIPLNT GTRKRIWQML GNSEEVAEFL LPKLGLTDAH
PADLEAVPYK SVPQWNDPMY RREVPFRINP KKTPFYIRRK STNEPVVFAK FIGKDLFGDF
QFHQLKKFEK YFPDILAYQD GYVMTKYEPG LKEMREMFVN MPSAVTREIC QSVSGYWKTL
LDSCQISGGH PVHPLADHWQ ARLGEMEDFI GRKLPYDLDW FERSLHTEWT SSAHVYTSLP
YANQYGHWKA RLSAGQRLKT YRFHIDSTWG GTSSIEVELA SFLLENRVRP DDFRLLVNQV
KKEAGSLTIE AVTDALPIAC VLQAANLLKQ AKDESRLSKE LILSEAMQSF EYLQAMKPKL
SDVR