ID G0WV61_STRVR Unreviewed; 526 AA.
AC G0WV61;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative choline dehydrogenase {ECO:0000313|EMBL:AEG64677.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:AEG64677.1};
RN [1] {ECO:0000313|EMBL:AEG64677.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 29814 {ECO:0000313|EMBL:AEG64677.1};
RA Yin X.H.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG64677.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 29814 {ECO:0000313|EMBL:AEG64677.1};
RX PubMed=21640802; DOI=10.1016/j.gene.2011.05.005;
RA Wang Y., Chen Y., Shen Q., Yin X.;
RT "Molecular cloning and identification of the laspartomycin biosynthetic
RT gene cluster from Streptomyces viridochromogenes.";
RL Gene 483:11-21(2011).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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; HM756254; AEG64677.1; -; Genomic_DNA.
DR AlphaFoldDB; G0WV61; -.
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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 206..308
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 396..516
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 136..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 57713 MW; DC788613DCBC568D CRC64;
MAGDQHYDVV IIGTGAGGGT LAHSLAPTGK RILILERGDY LPRERDNWDS TAVFVKGKYR
APEFWFDKHG NEFPPEVNYY VGGNTKFYGA ALFRLRPEDF GELRHHDGIS PAWPIRYEDM
EPYYTQAEQL YLVHGRHGED PTEGPASGPY PHPPVAHEPR IQQLSDDLEK EGLHPFHLPI
GVNLSQDDDG RATHSSVCIR CDRVDGFPCL VGAKSDAQVI CVDPALKHHN VTLLTGANVR
RLETDESGHT VTRVVAELGD GTTERFSAGI VVVACGAVNS AVLLLRSANE RHPNGLANGS
GVVGRHYMRH NNLALMAVSK EPNPTKFQKT LALHDWYLGA DDWDYPLGGI QMLGKSDADQ
IHGEAPRWAG AAAPDMPFEM LAHHAVDFWL CGEDLPRPEN RVTLDGNDAI HLALDEKNNI
AGLRRLQHKL QGMLSRLGMH EHHLLSHSIY LHKGMPIGAT AHQAGTVRFG DDPGSSALDV
NCKAHELDNL YVVDTSFFPS IGAVNPSLTA MANALRVGDH IAARLR
//