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NEOL_STRFR
ID   NEOL_STRFR              Reviewed;         279 AA.
AC   Q53U10; Q4A4C8;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=2'-N-acetylparomamine deacetylase;
DE            EC=3.5.1.112;
DE   AltName: Full=2'''-acetyl-6'''-hydroxyneomycin C deacetylase;
DE            EC=3.5.1.113;
DE   AltName: Full=Neomycin biosynthesis protein 16;
DE            Short=Neo-16;
DE   AltName: Full=Neomycin biosynthesis protein L;
GN   Name=neoL; Synonyms=neo16, neoD;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC   8233 / NRRL B-1195 / VKM Ac-150;
RX   PubMed=16506694; DOI=10.1038/ja.2005.104;
RA   Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K.;
RT   "Biosynthesis of 2-deoxystreptamine by three crucial enzymes in
RT   Streptomyces fradiae NBRC 12773.";
RL   J. Antibiot. 58:766-774(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC   8233 / NRRL B-1195 / VKM Ac-150;
RX   PubMed=15827636; DOI=10.1039/b501199j;
RA   Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y., Spencer J.B.;
RT   "The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233:
RT   characterisation of an aminotransferase involved in the formation of 2-
RT   deoxystreptamine.";
RL   Org. Biomol. Chem. 3:1410-1418(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC   8233 / NRRL B-1195 / VKM Ac-150;
RA   Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
RA   Welzel K., Vente A.;
RT   "Analysis and comparison of biosynthetic gene clusters for the 2-deoxy-
RT   inosamine containing aminoglycoside antibiotics ribostamycin, neomycin,
RT   lividomycin, paromomycin and butirosin.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC   8233 / NRRL B-1195 / VKM Ac-150;
RA   Subba B., Kharel M.K., Sthapit B., Liou K., Lee H.C., Woo J.S., Sohng J.K.;
RT   "Cloning and characterization of a neomycin biosynthetic gene cluster from
RT   Streptomyces fradiae, ATCC 10745.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=18311744; DOI=10.1002/cbic.200700717;
RA   Yokoyama K., Yamamoto Y., Kudo F., Eguchi T.;
RT   "Involvement of two distinct N-acetylglucosaminyltransferases and a dual-
RT   function deacetylase in neomycin biosynthesis.";
RL   ChemBioChem 9:865-869(2008).
CC   -!- FUNCTION: Deacetylase involved in the biosynthesis of neomycin by
CC       mediating 2 steps of the pathway. Deacetylates both 2'-N-
CC       acetylparomamine and 2'''-acetyl-6'''-hydroxyneomycin C.
CC       {ECO:0000269|PubMed:18311744}.
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:18311744};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'''-acetyl-6'''-hydroxyneomycin C + H2O = 6'''-deamino-6'''-
CC         hydroxyneomycin C + acetate; Xref=Rhea:RHEA:34051, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:65030, ChEBI:CHEBI:65031;
CC         EC=3.5.1.113; Evidence={ECO:0000269|PubMed:18311744};
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; neomycin biosynthesis.
CC       {ECO:0000269|PubMed:18311744}.
CC   -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH05093.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB211959; BAD95829.1; -; Genomic_DNA.
DR   EMBL; AJ843080; CAH58699.1; -; Genomic_DNA.
DR   EMBL; AJ629247; CAF33321.1; -; Genomic_DNA.
DR   EMBL; AJ786317; CAH05093.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q53U10; -.
DR   SMR; Q53U10; -.
DR   KEGG; ag:BAD95829; -.
DR   BioCyc; MetaCyc:MON-17259; -.
DR   UniPathway; UPA00969; -.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901158; P:neomycin 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   Pfam; PF02585; PIG-L; 1.
DR   SUPFAM; SSF102588; SSF102588; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Hydrolase; Metal-binding; Transferase; Zinc.
FT   CHAIN           1..279
FT                   /note="2'-N-acetylparomamine deacetylase"
FT                   /id="PRO_0000421745"
FT   REGION          245..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   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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