ID   LIVQ_STRLV              Reviewed;         546 AA.
AC   Q2MF66;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=6'''-hydroxyparomomycin C oxidase;
DE            EC=1.1.3.-;
DE   AltName: Full=Lividomycin biosynthesis protein Q;
GN   Name=livQ;
OS   Streptomyces lividus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=282216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=CBS 844.73;
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 lividomycin by mediating FAD-dependent dehydrogenation of 6'''-
CC       hydroxyparomomycin to paromomycin. {ECO:0000269|PubMed:21689223}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; lividomycin biosynthesis.
CC       {ECO:0000269|PubMed:21689223}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AJ748832; CAG38701.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF66; -.
DR   SMR; Q2MF66; -.
DR   KEGG; ag:CAG38701; -.
DR   BioCyc; MetaCyc:MON-17269; -.
DR   BRENDA; 1.1.3.44; 13009.
DR   UniPathway; UPA00968; -.
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:0017000; P:antibiotic 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..546
FT                   /note="6'''-hydroxyparomomycin C oxidase"
FT                   /id="PRO_0000421738"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        475
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   546 AA;  58907 MW;  249969633EF22C38 CRC64;
     MERLRGPSPL ENTTARHPAP LGPAHRDGLE PGTADRVWDV CVIGSGASGA VAADRLVRQG
     LDVLMVEEGF RLAPHVGLDE AESLSRQALA RDGEGNWTDE GWPWTTSNLG GGTVYYGGAS
     FRYRPFDFDP GELVHTDGVD VRWPYTLADL VPYYEVLERR LGVCGGDAPG IHRGSRHSRG
     PAHQPSPAAR VLRAAGESLG YRPFPTPLAI NRDPHGGRAA CARDSLCVSH LCPTGAKGDV
     VAVFLAPLAA HPNFALRTGV RALRLEQDRS GEVAAVRCLD RQTGQAHRVR ARVYVVACNA
     IQSAALLLRS RTPYSPDGVG NHSHLVGRGL CMKLSEYLSG TVDADPAVLA DPYTNTGPFS
     TVAFLDHYLD PDCPGGFGGL IYESKRDQRH KLVHDALELR IETILADHPN LDNRVGLSTH
     LDEDGMPAVV IDYTPDPRDL DRLRYMTGRC ERLLRTAGAR GIRSRSTGFA QGSSHLHGTC
     RAGHDPARSV VDAWGRVHSA DNVYIVDGSF MPYPGGLNPT LTIQAHALRT SRAIASHLAA
     DRAAHV