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Database: UniProt
Entry: A0A0H4CF47_9ACTN
LinkDB: A0A0H4CF47_9ACTN
Original site: A0A0H4CF47_9ACTN 
ID   A0A0H4CF47_9ACTN        Unreviewed;       520 AA.
AC   A0A0H4CF47;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AKN74592.1};
GN   ORFNames=QR97_37050 {ECO:0000313|EMBL:AKN74592.1};
OS   Streptomyces sp. PBH53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN74592.1, ECO:0000313|Proteomes:UP000036399};
RN   [1] {ECO:0000313|EMBL:AKN74592.1, ECO:0000313|Proteomes:UP000036399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBH53 {ECO:0000313|EMBL:AKN74592.1,
RC   ECO:0000313|Proteomes:UP000036399};
RX   PubMed=26227608;
RA   Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT   "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT   Urban Environment.";
RL   Genome Announc. 3:e00859-e00815(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA   Gosse J.T., Boddy C.N., Hill P.B.;
RT   "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT   urban environment.";
RL   Submitted (JUN-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}.
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DR   EMBL; CP011799; AKN74592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H4CF47; -.
DR   STRING; 1577075.QR97_37050; -.
DR   PATRIC; fig|1577075.3.peg.7792; -.
DR   Proteomes; UP000036399; Chromosome.
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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036399}.
FT   DOMAIN          252..266
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   520 AA;  54783 MW;  A6ADD628FE955435 CRC64;
     MSTYDYVIVG AGAAGCVLAA RLSEDPDVRV ALIEAGGPDS AQEIHVPAAF PQLFKSDLDW
     DLDSDPEPGL GGRRTYLPRG RMFGGSSSMN AMIYIRGSRA DYDGWAAAGA TGWSYAEVLP
     YFKRSEDNER GEDAFHGVGG PLTVSDGRSD HPLATAFVQA AVEAGHKAND DFNGETQFGV
     GRYQLTQRGG MRCSTAVAFL HPALERPNLT VLSSARAHRV VIEGGRAVGV EVERGGTVDT
     VRAEREVILS AGAYESPKLL MLSGIGPAAD LSAFGIDVVR DLPVGQGLQD HYMTLLNFRT
     AAESLISAAT PENAALLQNE GRGPLTSNIG EAGGFFRSRD GLDAPDLQFH AAPSLFHQEG
     LGAATEHGFA FGPCVLAPTS RGAVTLRSPR PDVAPRIVHN YLTTAEDQDA IVAGIRIALD
     IAAQRAVTDL ATGLYGDTPA ASASDADLLA WARRSGQTLY HPTSTCAIGS VVDPELRVYD
     VPGLRVVDAS VFPTVTRGNT NAPTVMAAEK AADLIRGAVR
//
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