ID A0A0C4YLM7_9BURK Unreviewed; 535 AA.
AC A0A0C4YLM7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AJG23470.1};
DE EC=1.1.99.1 {ECO:0000313|EMBL:AJG23470.1};
GN ORFNames=RR42_s1882 {ECO:0000313|EMBL:AJG23470.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG23470.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG23470.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG23470.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(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}.
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DR EMBL; CP010537; AJG23470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4YLM7; -.
DR STRING; 68895.RR42_s1882; -.
DR KEGG; cbw:RR42_s1882; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000031843; Chromosome secondary.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; 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 Oxidoreductase {ECO:0000313|EMBL:AJG23470.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 257..271
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 501
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 535 AA; 58303 MW; 1FF007F4A0554339 CRC64;
MKTATYDYIV IGAGSAGCVL ASRLSEDPSV KVLLIEAGAP ASSIFVQMPA GIRVLYKSQK
FNWRYWTEPQ TQLDNRNIYI PRGKVVGGSS SINSMIAIRG NRSDYDNWAS QGLSGWDYES
LRPYFRKIED ASLVTKARND DRGYAGPIRL SYGTQQNAIS TAFIESAVSA GMPENNGFNG
ASQVGAGFYE LTIAEGKRSG AYRYLDRAGN RSNLTLMANC KVRRILLAGK RAQGVVIEDG
WEEVELRADR EVILTAGAIA SPQLLMLSGI GPAKHLQSIG IAPVVDLQGV GENLQDHLDC
AIRLEASQPN TLTPYIGLVR GGMAGARYLL SGGGPASSQG VEAGAFYNSD RNPDLPEWQA
HLIIALRNPP PNEKVPHGFA VRVCQLRPKS RGVLRLRSSD PSDSPRIDPR FLSDESDLES
LVRGVERTCE IVDQPALRKY IKRRLDIDAF STGAARKAWI RSHAETIYHP VGTCRMGVDD
NAVVDEELKV RGVENLRVID GSVMPTIISG NTNLPIMAMA EKAADLIRNS RTSAR
//