ID A0A0S8BBK1_9PROT Unreviewed; 531 AA.
AC A0A0S8BBK1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KPK09008.1};
GN ORFNames=AMJ64_01745 {ECO:0000313|EMBL:KPK09008.1};
OS Betaproteobacteria bacterium SG8_39.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK09008.1, ECO:0000313|Proteomes:UP000051483};
RN [1] {ECO:0000313|EMBL:KPK09008.1, ECO:0000313|Proteomes:UP000051483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_39 {ECO:0000313|EMBL:KPK09008.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPK09008.1}.
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DR EMBL; LJTQ01000007; KPK09008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BBK1; -.
DR STRING; 1703390.AMJ64_01745; -.
DR PATRIC; fig|1703390.3.peg.3252; -.
DR Proteomes; UP000051483; 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; 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.
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}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 253..267
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 94..97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 531 AA; 58374 MW; BF3F32FBAFA2F249 CRC64;
MTDTTTYDYI IVGAGSAGCV LANRLTANGR HRVLLLEAGP RDTDFWIHVP LGYGKLFTRT
DVNWAYEGEP EPNLNGRRVF TPRGKVLGGS SSINGLVYIR GQREDFDGWG VPGWGFDDLL
PYFRKSEDQS RGADAWHGVG GPLAVSDLPD KHELCEAFID SAQALGVPQN DDFNGANQEG
TGYYQATARN GRRCSTATGY LRPAEKRPNL RVEVEALATR ILFEGSRASG IEYRQRGATH
AARAAREVIL AGGTFNSPQL LQLSGVGPRA LLEPHGISMV RDVPEVGENL QDHLYVRTFW
RCNKAITLND DMMSWWRQAK IGLQYLLFKR GPLTVSAGYA AAFVRTRPEL ARPDAQLYFI
NFSTAKRGGY LHPFSGFTCS VSQLQAESRG WVRLRDADPA SPPAILYNYL AAEADRRMMV
EGLKFARRLV NTPPLSGYVV NEEHPGPRVQ SDDEWLAFCR EAGDTVFHPT STCRMGTDDR
SVVDPRLRVR GLEGLRVVDA SVMPAVPSGN INAAVIAVAE KGADLVLEDA G
//
