ID   NEOG_STRFR              Reviewed;         541 AA.
AC   Q53U15;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Paromamine 6'-oxidase;
DE            EC=1.1.3.43 {ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223};
DE   AltName: Full=6'''-hydroxyneomycin C oxidase;
DE            EC=1.1.3.44 {ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223};
DE   AltName: Full=Neomycin biosynthesis protein 11;
DE            Short=Neo-11;
DE   AltName: Full=Neomycin biosynthesis protein Q;
GN   Name=neoG; Synonyms=nemG, neo11, neoQ;
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, COFACTOR, AND PATHWAY.
RC   STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC   8233 / NRRL B-1195 / VKM Ac-150;
RX   PubMed=17206729; DOI=10.1002/cbic.200600371;
RA   Huang F., Spiteller D., Koorbanally N.A., Li Y., Llewellyn N.M.,
RA   Spencer J.B.;
RT   "Elaboration of neosamine rings in the biosynthesis of neomycin and
RT   butirosin.";
RL   ChemBioChem 8:283-288(2007).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21689223; DOI=10.1111/j.1365-2672.2011.05082.x;
RA   Clausnitzer D., Piepersberg W., Wehmeier U.F.;
RT   "The oxidoreductases LivQ and NeoQ are responsible for the different 6'-
RT   modifications in the aminoglycosides lividomycin and neomycin.";
RL   J. Appl. Microbiol. 111:642-651(2011).
CC   -!- FUNCTION: Glucosaminyl-6'-oxidase involved in the biosynthetic pathway
CC       of neomycin by mediating FAD-dependent dehydrogenation of paromamine to
CC       6'-dehydro-6'-oxoparomamine. Works in combination with neamine
CC       transaminase to replace the 6-hydroxy group of paromamine with an amino
CC       group. Also able to collaborate with neomycin C transaminase to replace
CC       the 6'''-hydroxy group of 6'''-hydroxyneomycin C with an amino group.
CC       {ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6'''-deamino-6'''-hydroxyneomycin C + O2 = 6'''-deamino-6'''-
CC         oxoneomycin C + H2O2; Xref=Rhea:RHEA:34047, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:65031, ChEBI:CHEBI:65068; EC=1.1.3.44;
CC         Evidence={ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + paromamine = 6'-oxoparomamine + H2O2;
CC         Xref=Rhea:RHEA:34035, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:65015, ChEBI:CHEBI:65016; EC=1.1.3.43;
CC         Evidence={ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:17206729};
CC   -!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
CC       {ECO:0000269|PubMed:17206729}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AB211959; BAD95824.1; -; Genomic_DNA.
DR   EMBL; AJ843080; CAH58694.1; -; Genomic_DNA.
DR   EMBL; AJ629247; CAF33316.1; -; Genomic_DNA.
DR   EMBL; AJ786317; CAH05097.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53U15; -.
DR   SMR; Q53U15; -.
DR   KEGG; ag:BAD95824; -.
DR   BioCyc; MetaCyc:MON-17237; -.
DR   BRENDA; 1.1.3.43; 5932.
DR   BRENDA; 1.1.3.44; 5932.
DR   UniPathway; UPA00969; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA:UniProtKB.
DR   GO; GO:1901158; P:neomycin biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..541
FT                   /note="Paromamine 6'-oxidase"
FT                   /id="PRO_0000421737"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        470
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   541 AA;  58004 MW;  49172B03C8AD198A CRC64;
     MKRLRGTLPS DARHAWHPEP LGPAHRDGWD TRDDDRVWDV VVIGSGASGS VAADRLVRQG
     LDVLMIEEGF RLSPDLGNPE LDDMCRTALA RDGQGGWTDE GWPWTTSNLG GGTVFYGGAS
     WRYRPFDFDP SELVDAGGLD VRWPYGLAEL APYYDVLERR LGVCGGEEGE GSRGPAHPPT
     AAAEVLYEAG TALGYEPFPT PLAINRHAHG GRSACERNSL CVSHQCSTGA KGDAVAVFLA
     PLAAHPNFTL RTGVRALRLN QDRPDAVGSV TCLDRLGRTT HRVRARSFVV ACNAIQSAAL
     LLRSRGGRAP DGVGNHSGLV GRGLTMKLSE YVSGVVDAPS AATLADWRAH AGPFSTIAFL
     DHYLDADCPT GVGGMIYESK NDMPSRIRDD VLELRIETIL ADHPNLDNRV RLSSHADEDG
     VPAVVIDYTP DPRDLRRLAY MTDVCERLLR KAGATGIAHE ESGFAQGSCH LHGTCRAGDD
     PATSVVDGWG RVHSAPNVYV VDGGFMPYPG GLNPTLTIQA HALRSAKAVA GDLVSRHTAH
     V