ID A0A0N1NQ70_9ACTN Unreviewed; 489 AA.
AC A0A0N1NQ70;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KPI23267.1};
DE EC=1.1.99.1 {ECO:0000313|EMBL:KPI23267.1};
GN ORFNames=OV320_0782 {ECO:0000313|EMBL:KPI23267.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI23267.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI23267.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI23267.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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}.
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:KPI23267.1}.
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DR EMBL; LJCX01000033; KPI23267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NQ70; -.
DR PATRIC; fig|1592329.3.peg.8567; -.
DR Proteomes; UP000037870; Unassembled WGS sequence.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 2.
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, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000313|EMBL:KPI23267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT DOMAIN 237..251
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 203
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 424..425
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 489 AA; 51982 MW; 2AFCDE84CB9DE25C CRC64;
MTLPDHATIV VLGGGTAGCV VAARLARHHD VLVLEAGPDY GPERASWPAE LLDASTLPTT
HDWGYREGRL TFDRCRVIGG CSTHNGCTQS VGWAGDYDAW AASGSPGWDA ASLAPYFREV
ERTLRFRRYG EDEIQPFQRA FIGAAEKLGV PARDDLDDLR AGASVGCAPV NVTPGGVRVN
TAFGYLDPMR GSGNLTVAGG VTVDRVVLDG GRAVAVDVLT DQGARRIAAD LIVVAAGAYG
TPEILLRSGI GPADHLGETG VPVLHHLPGV GANLHDQPAV NLQYAASAAL AADLEAFAET
RMLPDEQALA KLRSPYAGNA PYDLHVYPWT ERDATLEHGW RIVVPVGLLR PKSRGTVRLR
SADPTVRAAV DHAFLTHPDD LAALVHGVSR AQELDLAHYL SAELPAPPVD GLPDWIRATH
QHYWHPAGSC RMGPADDPDA VVDHTGKVHG LEGLHIADAS VFPDIPRGTP AHPTAVVGER
MASFLEELL
//
