ID A0A221SVZ7_9DEIO Unreviewed; 527 AA.
AC A0A221SVZ7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:ASN80826.1};
GN ORFNames=DFI_07245 {ECO:0000313|EMBL:ASN80826.1};
OS Deinococcus ficus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=317577 {ECO:0000313|EMBL:ASN80826.1, ECO:0000313|Proteomes:UP000259030};
RN [1] {ECO:0000313|EMBL:ASN80826.1, ECO:0000313|Proteomes:UP000259030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-FR2-10 {ECO:0000313|EMBL:ASN80826.1,
RC ECO:0000313|Proteomes:UP000259030};
RA Wu K.-M., Liao T.-L., Liu Y.-M., Young C.-C., Tsai S.-F.;
RT "The complete genome sequence of Deinococcus ficus isolated from the
RT rhizosphere of the Ficus religiosa L. in Taiwan.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CP021081; ASN80826.1; -; Genomic_DNA.
DR RefSeq; WP_027461591.1; NZ_CP021081.1.
DR AlphaFoldDB; A0A221SVZ7; -.
DR STRING; 317577.GCA_000419625_02469; -.
DR KEGG; dfc:DFI_07245; -.
DR Proteomes; UP000259030; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000259030}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 252..266
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 527 AA; 56021 MW; E376E1CE8B728DA5 CRC64;
MTGQLGRRAD VIVVGAGSGG CVLARRLLDR GLRVLLLEAG ERDGSPLIRA PAAFPRLYRS
RYDWAFETVP QAHADGRRFF WPRGKVLGGS SAINATIWIR GSRRDFDAWG EGWRWADVLP
AFRTLERFSG TPGDTRGTDG PLPVGLRRDS HALSHAFVQS AARALGVPAA ASFNDGTLAG
AALLESNHLR GERFSAFRAF LRPVLSHPNL TVLTGAHVLR VLFQGTRAVG VRLRWQGRTL
DAPAGGVVLT AGAVQTPQLL LLSGVGPLGE LARHGIEPVA AVPGVGVGLQ DHPAIPVIYR
SGTPSLEAMP ELEALARYAL TRRGPLSSNV AEACAFTHAR ADLNPAQDDP DIQFLFGPAY
FRDHGFRKAP GHHFSVGPVL VDVHSRGRIT LASRDPRAAP LIDPAYFSDE RDMRSMVSGI
RLAREIAGAP PLAGHARGEA VPGAAVQSVG ALRAYLRAEA ATLYHPTSTA VLGDGPEAVV
DRQLAVRDTA GLWVADASVM PRVIHANTNA TSMMIGERAA AFVAGGL
//
