ID H1SBQ2_9BURK Unreviewed; 494 AA.
AC H1SBQ2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Choline dehydrogenase, a flavoprotein {ECO:0000313|EMBL:EHP40044.1};
GN ORFNames=OR16_28089 {ECO:0000313|EMBL:EHP40044.1};
OS Cupriavidus basilensis OR16.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP40044.1, ECO:0000313|Proteomes:UP000005808};
RN [1] {ECO:0000313|EMBL:EHP40044.1, ECO:0000313|Proteomes:UP000005808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR16 {ECO:0000313|EMBL:EHP40044.1,
RC ECO:0000313|Proteomes:UP000005808};
RX PubMed=22461549; DOI=10.1128/JB.06752-11;
RA Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
RA Nagy I., Horvath B., Nagy I., Kukolya J.;
RT "De Novo Genome Project of Cupriavidus basilensis OR16.";
RL J. Bacteriol. 194:2109-2110(2012).
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:EHP40044.1}.
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DR EMBL; AHJE01000075; EHP40044.1; -; Genomic_DNA.
DR RefSeq; WP_006161222.1; NZ_AHJE01000075.1.
DR AlphaFoldDB; H1SBQ2; -.
DR PATRIC; fig|1127483.3.peg.5604; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000005808; 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; 2.
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}.
FT DOMAIN 95..118
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 275..289
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 494 AA; 52819 MW; 268FDAC247FA663A CRC64;
MSNAAKPPHR QSPAAEYDYL VVGAGSAGCA LAARLAEDPA VTVALLEAGP DDHHYSVWTP
LALAAVVPKP GPRNYAYRTV AQAGLGGRRS YQPRGRGLGG SSSINGMVYI RGHRHDYDDW
ERLGCTGWGF DDVLPYFRRS ERNQRLSDAH HGSDGPLHVS DLRTPNPFSQ RFVAAAVQAG
VPLNVDFNGA QQEGAGLYQV TQRNGERWNS ARAYLHGGNA ADTGLNGGRR GLTVLTETQA
LRVVFEGKRA TGVHVSRAGA EQTLRARREV ILSSGAFNSP QLLLASGIGP ASHLCGHGIA
VIHDLPGVGE NLQDHLDITV CQQVRTTDLF GYSLGGVFRM LSEIRRYRRD RTGMVSSNLA
EAGAFIKSRP GLAEPDLQLH FMPGLSPTHT GLSRRELKHG FTGLACVLRP QSRGHVRLES
ADTRDAPLID PRFLSAEADM AGMVAGVRAL RRIFSQQALA GAGGTELLTG AFGAGAPAIM
IGEKAADLIR AANR
//