ID   BTRP_NIACI              Reviewed;         213 AA.
AC   Q4H4E4;
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=5''-phosphoribostamycin phosphatase;
DE            EC=3.1.3.88;
DE   AltName: Full=Butirosin biosynthesis protein P;
GN   Name=btrP;
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=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 dephosphorylation of 5''-phosphoribostamycin to
CC       generate ribostamycinin the biosynthetic pathway of butirosin.
CC       {ECO:0000269|PubMed:17482823}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5''-phosphoribostamycin + H2O = phosphate + ribostamycin;
CC         Xref=Rhea:RHEA:33971, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:65028, ChEBI:CHEBI:65082; EC=3.1.3.88;
CC         Evidence={ECO:0000269|PubMed:17482823};
CC   -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC       {ECO:0000269|PubMed:17482823}.
CC   -!- SIMILARITY: Belongs to the histidine phosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB097196; BAE07077.1; -; Genomic_DNA.
DR   EMBL; AJ781030; CAG77431.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H4E4; -.
DR   SMR; Q4H4E4; -.
DR   KEGG; ag:BAE07077; -.
DR   BioCyc; MetaCyc:MON-17255; -.
DR   UniPathway; UPA00964; -.
DR   GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Hydrolase.
FT   CHAIN           1..213
FT                   /note="5''-phosphoribostamycin phosphatase"
FT                   /id="PRO_0000421729"
FT   ACT_SITE        8
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000250"
FT   SITE            62
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  24505 MW;  88D424FA7FB12DE0 CRC64;
     MRLILIRHAQ ARCNILEDDA LMDAYDPHCE LTEAGIGQAV KLRDEYPVSL TPSVIYSSPL
     KRARETAGIF RGRYPSVPFV EDERLSELKA PESFIPPITQ GQWDLYLEQR IRSPHLEIVK
     GLESLDVQRE RIERFYKDLF RKYAEEACNI VIFTHAFSIQ LSILFFLGLG NEQLLQWQIK
     ASNTAMHIIH YDPTSGSFLL ESLNNRSHLQ TTG