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2'-N-acetylparomamine deacetylase (EC 3.5.1.112) (2'''-acetyl-6'''-hydroxyneomycin C deacetylase) (EC 3.5.1.113) (Neomycin biosynthesis protein 16) (Neo-16) (Neomycin biosynthesis protein L)

 NEOL_STRFR              Reviewed;         279 AA.
Q53U10; Q4A4C8;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
22-NOV-2017, entry version 42.
RecName: Full=2'-N-acetylparomamine deacetylase;
EC=3.5.1.112;
AltName: Full=2'''-acetyl-6'''-hydroxyneomycin C deacetylase;
EC=3.5.1.113;
AltName: Full=Neomycin biosynthesis protein 16;
Short=Neo-16;
AltName: Full=Neomycin biosynthesis protein L;
Name=neoL; Synonyms=neo16, neoD;
Streptomyces fradiae (Streptomyces roseoflavus).
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1906;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
PubMed=16506694; DOI=10.1038/ja.2005.104;
Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K.;
"Biosynthesis of 2-deoxystreptamine by three crucial enzymes in
Streptomyces fradiae NBRC 12773.";
J. Antibiot. 58:766-774(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
PubMed=15827636; DOI=10.1039/b501199j;
Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y.,
Spencer J.B.;
"The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB
8233: characterisation of an aminotransferase involved in the
formation of 2-deoxystreptamine.";
Org. Biomol. Chem. 3:1410-1418(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
Welzel K., Vente A.;
"Analysis and comparison of biosynthetic gene clusters for the 2-
deoxy-inosamine containing aminoglycoside antibiotics ribostamycin,
neomycin, lividomycin, paromomycin and butirosin.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
Subba B., Kharel M.K., Sthapit B., Liou K., Lee H.C., Woo J.S.,
Sohng J.K.;
"Cloning and characterization of a neomycin biosynthetic gene cluster
from Streptomyces fradiae, ATCC 10745.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=18311744; DOI=10.1002/cbic.200700717;
Yokoyama K., Yamamoto Y., Kudo F., Eguchi T.;
"Involvement of two distinct N-acetylglucosaminyltransferases and a
dual-function deacetylase in neomycin biosynthesis.";
ChemBioChem 9:865-869(2008).
-!- FUNCTION: Deacetylase involved in the biosynthesis of neomycin by
mediating 2 steps of the pathway. Deacetylates both 2'-N-
acetylparomamine and 2'''-acetyl-6'''-hydroxyneomycin C.
{ECO:0000269|PubMed:18311744}.
-!- CATALYTIC ACTIVITY: 2'-N-acetylparomamine + H(2)O = paromamine +
acetate. {ECO:0000269|PubMed:18311744}.
-!- CATALYTIC ACTIVITY: 2'''-acetyl-6'''-deamino-6'''-hydroxyneomycin
C + H(2)O = 6'''-deamino-6'''-hydroxyneomycin C + acetate.
{ECO:0000269|PubMed:18311744}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
{ECO:0000269|PubMed:18311744}.
-!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAH05093.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB211959; BAD95829.1; -; Genomic_DNA.
EMBL; AJ843080; CAH58699.1; -; Genomic_DNA.
EMBL; AJ629247; CAF33321.1; -; Genomic_DNA.
EMBL; AJ786317; CAH05093.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; Q53U10; -.
KEGG; ag:BAD95829; -.
KO; K17078; -.
BioCyc; MetaCyc:MONOMER-17259; -.
UniPathway; UPA00969; -.
GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:1901158; P:neomycin biosynthetic process; IDA:UniProtKB.
Gene3D; 3.40.50.10320; -; 1.
InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
InterPro; IPR024078; LmbE-like_dom_sf.
PANTHER; PTHR12993; PTHR12993; 1.
Pfam; PF02585; PIG-L; 1.
SUPFAM; SSF102588; SSF102588; 1.
1: Evidence at protein level;
Antibiotic biosynthesis; Hydrolase; Metal-binding; Transferase; Zinc.
CHAIN 1 279 2'-N-acetylparomamine deacetylase.
/FTId=PRO_0000421745.
METAL 31 31 Zinc. {ECO:0000250}.
METAL 34 34 Zinc. {ECO:0000250}.
METAL 157 157 Zinc. {ECO:0000250}.
SEQUENCE 279 AA; 30109 MW; 9E69F7930B40152A CRC64;
MGEPTWEAAE DPDRTLRERL RRGRTLLVSP HPDDVAYSCG GLLAAVGRPA HATLLTVFTR
SAWALPRRLR RAGARVVSER RREEELRYCR LRGLAEYRPL GFADAGLRGY DDETELSSPA
EADGVRGAVE EAVAEAIRDA GADTVLAPAA VGGHVDHLLV HGAVRGAVGP GGPLTLFYED
LPYAGQRDAV DVERTLREAR GLVPFASVDI SGVVQQKVRG MYVYGSQTDD ECVRETLRHA
RRGAPRRWTG GTAGAGHAAG RRGAPHTERV WTPAPAGAR


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