ID A0A0W0VTK5_9GAMM Unreviewed; 451 AA.
AC A0A0W0VTK5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=6'''-hydroxyparomomycin C oxidase {ECO:0000313|EMBL:KTD23520.1};
DE EC=1.1.3.- {ECO:0000313|EMBL:KTD23520.1};
GN Name=livQ {ECO:0000313|EMBL:KTD23520.1};
GN ORFNames=Llan_0778 {ECO:0000313|EMBL:KTD23520.1};
OS Legionella lansingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD23520.1, ECO:0000313|Proteomes:UP000054869};
RN [1] {ECO:0000313|EMBL:KTD23520.1, ECO:0000313|Proteomes:UP000054869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD23520.1,
RC ECO:0000313|Proteomes:UP000054869};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTD23520.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYI01000013; KTD23520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VTK5; -.
DR STRING; 45067.Llan_0778; -.
DR PATRIC; fig|45067.4.peg.808; -.
DR eggNOG; COG2303; Bacteria.
DR Proteomes; UP000054869; 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; IPR006076; FAD-dep_OxRdtase.
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; PF01266; DAO; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:KTD23520.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054869}.
FT DOMAIN 5..36
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 194..259
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 340..438
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 451 AA; 50826 MW; 22C9DAF4CBF1B1CC CRC64;
MEHEVTIIGS GILGAVCAHH LAKKGVKVLI LEAGAPISTP PGEHLRNQQK YREHPDQFFD
EIETYCQLFD VDAPPEGLPG ANITHAYGGQ ATLWTNNCPR PARHEQWPEF DDMNMNEYLS
RAENILHVQK DLFDCSIRQM NLFAAIDPIL RIQNRSLAKV PLAGRKRKNN DIEFTSTLQI
LDLPKEVREL ITIQMNTEVI ELLHNKSTIS GLKVKQNQQL KDIKANRIII AAGAFDTTQL
LYNSHIHSAA LGHYLHFHPL HLAQVVLNSS LVATDEIADI PPRTCIYPTP NYPWHAMILR
DIFPNVSTEV IDENKLIDFQ YFVPIDVQEK NRMILSKDKP KFEVRLTDND KQIIDAAMKD
LKSLANHLGR YRKGCEPRSM DFGFTHPMGV CRMGTDVSNS VTNLKGKVHG FNNLYLATVG
LIPTKMAVNP TLTAAALALI TTDYITEEGF R
//
