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Database: UniProt
Entry: A0A0L6CRL8_9RHOB
LinkDB: A0A0L6CRL8_9RHOB
Original site: A0A0L6CRL8_9RHOB 
ID   A0A0L6CRL8_9RHOB        Unreviewed;       525 AA.
AC   A0A0L6CRL8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=6'''-hydroxyparomomycin C oxidase {ECO:0000313|EMBL:KNX40356.1};
DE            EC=1.1.3.- {ECO:0000313|EMBL:KNX40356.1};
GN   Name=livQ {ECO:0000313|EMBL:KNX40356.1};
GN   ORFNames=ROTO_31140 {ECO:0000313|EMBL:KNX40356.1};
OS   Roseovarius tolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX40356.1, ECO:0000313|Proteomes:UP000037046};
RN   [1] {ECO:0000313|Proteomes:UP000037046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA   Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT   "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT   Acylated Alanine Methyl Esters (NAMEs).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNX40356.1}.
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DR   EMBL; LGVV01000056; KNX40356.1; -; Genomic_DNA.
DR   RefSeq; WP_050663962.1; NZ_LGVV01000056.1.
DR   AlphaFoldDB; A0A0L6CRL8; -.
DR   STRING; 74031.SAMN04488077_104263; -.
DR   PATRIC; fig|74031.6.peg.3181; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000037046; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:KNX40356.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037046}.
FT   DOMAIN          82..302
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          402..512
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   525 AA;  57073 MW;  A4CFC99BF8C2CD2C CRC64;
     MSSDIRDTLW DVIVIGAGMG GGIIGRRLAE RGLKVLFVEK GPQGYRAERQ GLDPEMGDPV
     ARQLRGYWPG RVRARIDGRA SEFFGPLGAG VGGSSVFYAA TLERPERHDL EPVEGRPHPT
     GGWPVGYDAM RDWYAEAEQL LHVCGAADPL SPEPVDPLRE PPPLSGVDRA LMHSLRGAGL
     HPYRLHSAIR YLEGCEGCLG RKCPRACKMD GRSAGVEPAL ATGRAALLDD CEVRRLCGGA
     DHVSHIEVTQ GGEAFELRAR QFVLAGGALG SPRLLLASAS EAWPEGCANG SGLVGRNLMF
     HLNEIFALWP PRGTPQDGPG KAISLRDFYH WQGQRFGTVQ AMGIAAGYGE IVHALNGMFD
     RSALRNLRAL RHLTRLPAAV AARLLGRAQV FVGLMEDLGY PENRVTWDAR APEVIDIDYT
     LNPELLARRR AFRRAIRAGL RGHRAFFLTH APELNFGHPC GTLRMGDDPD TSVLDAECRA
     HGIGNLYVAD SSFMPSSMGV NPSLTIAANA LRVAEVMVRR REGQE
//
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