ID   BTRD_NIACI              Reviewed;         275 AA.
AC   Q4H4F3;
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'-N-acetylparomamine deacetylase;
DE            EC=3.5.1.112;
DE   AltName: Full=Butirosin biosynthesis protein D;
GN   Name=btrD;
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   PRELIMINARY FUNCTION.
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).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17226887; DOI=10.1002/anie.200604194;
RA   Truman A.W., Huang F., Llewellyn N.M., Spencer J.B.;
RT   "Characterization of the enzyme BtrD from Bacillus circulans and revision
RT   of its functional assignment in the biosynthesis of butirosin.";
RL   Angew. Chem. Int. Ed. 46:1462-1464(2007).
CC   -!- FUNCTION: Deacetylase involved in the biosynthesis of butirosin by
CC       mediating deacetylation of 2'-N-acetylparomamine.
CC       {ECO:0000269|PubMed:17226887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-N-acetylparomamine + H2O = acetate + paromamine;
CC         Xref=Rhea:RHEA:34031, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:65010, ChEBI:CHEBI:65015; EC=3.5.1.112;
CC         Evidence={ECO:0000269|PubMed:17226887};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC   -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
CC   -!- CAUTION: Was initially thought to function as a nucleotidyltransferase
CC       (PubMed:15701005). But it was later shown that it is a deacetylase
CC       (PubMed:17226887). {ECO:0000305|PubMed:15701005,
CC       ECO:0000305|PubMed:17226887}.
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DR   EMBL; AB097196; BAE07068.1; -; Genomic_DNA.
DR   EMBL; AJ781030; CAG77422.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4H4F3; -.
DR   SMR; Q4H4F3; -.
DR   PRIDE; Q4H4F3; -.
DR   BioCyc; MetaCyc:MON-17232; -.
DR   UniPathway; UPA00964; -.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.10320; -; 1.
DR   InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR   InterPro; IPR024078; LmbE-like_dom_sf.
DR   PANTHER; PTHR12993; PTHR12993; 1.
DR   Pfam; PF02585; PIG-L; 1.
DR   SUPFAM; SSF102588; SSF102588; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..275
FT                   /note="2'-N-acetylparomamine deacetylase"
FT                   /id="PRO_0000421744"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  31822 MW;  03A6E77C242B6F61 CRC64;
     MNQDKRAFMF ISPHFDDVIL SCASTLMELM NQGHTCKVLT VFGGCPSVRF QPGEIARQYA
     AEDLGLFEDE IEGDHLSILV ARRLQEDQQA FRHLPGVQVE VLSFPDAIYR ENKGQPYYRT
     EADLFGIPDK QDEDIFLPKI ETYLQSCDLA RKYTWVFPAI SKHVDHRLLT KAGLRLMSQG
     YPVLFYSEFP YWQQHNEFLQ DGWRQLELRN SVYTPVKRAA VLEYKTQLLG LFGEEAETKI
     NNGGVLSEAE LFWIQETDTQ AWRVFRSLSP EPLQT