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Paromamine 6'-oxidase (EC 1.1.3.43) (6'''-hydroxyneomycin C oxidase) (EC 1.1.3.44) (Neomycin biosynthesis protein 11) (Neo-11) (Neomycin biosynthesis protein Q)

 NEOG_STRFR              Reviewed;         541 AA.
Q53U15;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
05-DEC-2018, entry version 61.
RecName: Full=Paromamine 6'-oxidase;
EC=1.1.3.43 {ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223};
AltName: Full=6'''-hydroxyneomycin C oxidase;
EC=1.1.3.44 {ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223};
AltName: Full=Neomycin biosynthesis protein 11;
Short=Neo-11;
AltName: Full=Neomycin biosynthesis protein Q;
Name=neoG; Synonyms=nemG, neo11, neoQ;
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, COFACTOR, AND PATHWAY.
STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 /
NCIMB 8233 / NRRL B-1195 / VKM Ac-150;
PubMed=17206729; DOI=10.1002/cbic.200600371;
Huang F., Spiteller D., Koorbanally N.A., Li Y., Llewellyn N.M.,
Spencer J.B.;
"Elaboration of neosamine rings in the biosynthesis of neomycin and
butirosin.";
ChemBioChem 8:283-288(2007).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=21689223; DOI=10.1111/j.1365-2672.2011.05082.x;
Clausnitzer D., Piepersberg W., Wehmeier U.F.;
"The oxidoreductases LivQ and NeoQ are responsible for the different
6'-modifications in the aminoglycosides lividomycin and neomycin.";
J. Appl. Microbiol. 111:642-651(2011).
-!- FUNCTION: Glucosaminyl-6'-oxidase involved in the biosynthetic
pathway of neomycin by mediating FAD-dependent dehydrogenation of
paromamine to 6'-dehydro-6'-oxoparomamine. Works in combination
with neamine transaminase to replace the 6-hydroxy group of
paromamine with an amino group. Also able to collaborate with
neomycin C transaminase to replace the 6'''-hydroxy group of 6'''-
hydroxyneomycin C with an amino group.
{ECO:0000269|PubMed:17206729, ECO:0000269|PubMed:21689223}.
-!- CATALYTIC ACTIVITY:
Reaction=6'''-deamino-6'''-hydroxyneomycin C + O2 = 6'''-deamino-
6'''-oxoneomycin C + H2O2; Xref=Rhea:RHEA:34047,
ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:65031,
ChEBI:CHEBI:65068; EC=1.1.3.44;
Evidence={ECO:0000269|PubMed:17206729,
ECO:0000269|PubMed:21689223};
-!- CATALYTIC ACTIVITY:
Reaction=O2 + paromamine = 6'-oxoparomamine + H2O2;
Xref=Rhea:RHEA:34035, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
ChEBI:CHEBI:65015, ChEBI:CHEBI:65016; EC=1.1.3.43;
Evidence={ECO:0000269|PubMed:17206729,
ECO:0000269|PubMed:21689223};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17206729};
-!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
{ECO:0000269|PubMed:17206729}.
-!- SIMILARITY: Belongs to the GMC oxidoreductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB211959; BAD95824.1; -; Genomic_DNA.
EMBL; AJ843080; CAH58694.1; -; Genomic_DNA.
EMBL; AJ629247; CAF33316.1; -; Genomic_DNA.
EMBL; AJ786317; CAH05097.1; -; Genomic_DNA.
ProteinModelPortal; Q53U15; -.
KEGG; ag:BAD95824; -.
KO; K20565; -.
BioCyc; MetaCyc:MONOMER-17237; -.
BRENDA; 1.1.3.43; 5932.
BRENDA; 1.1.3.44; 5932.
UniPathway; UPA00969; -.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA:UniProtKB.
GO; GO:1901158; P:neomycin biosynthetic process; IDA:UniProtKB.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR000172; GMC_OxRdtase_N.
InterPro; IPR007867; GMC_OxRtase_C.
Pfam; PF05199; GMC_oxred_C; 1.
Pfam; PF00732; GMC_oxred_N; 1.
SUPFAM; SSF51905; SSF51905; 1.
1: Evidence at protein level;
Antibiotic biosynthesis; FAD; Flavoprotein; Oxidoreductase.
CHAIN 1 541 Paromamine 6'-oxidase.
/FTId=PRO_0000421737.
ACT_SITE 470 470 Proton acceptor.
{ECO:0000250|UniProtKB:E4QP00}.
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


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