ID A0A0S1Y4V5_9BORD Unreviewed; 544 AA.
AC A0A0S1Y4V5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:ALM84950.1};
GN ORFNames=ASB57_20020 {ECO:0000313|EMBL:ALM84950.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM84950.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM84950.1, ECO:0000313|Proteomes:UP000064621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM84950.1,
RC ECO:0000313|Proteomes:UP000064621};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013111; ALM84950.1; -; Genomic_DNA.
DR RefSeq; WP_057653802.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y4V5; -.
DR STRING; 1746199.ASB57_20020; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000064621; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT DOMAIN 263..277
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 544 AA; 58613 MW; EF6F5AA5F80B192A CRC64;
MPAQLSEEFD YVVVGSGAAG AIVASRLSED PSVTVCLLEA GQRNWSPWLH IPAGFIKVVK
DPAWTWQFAA EPSARTAQRA IALPQGRTLG GTTSINGLIY NRGQAEDYLA WSALGVRGWT
YADVLPYFKR SERWVGGGDS EFHGRDGNIA VSRSPWRSTI CDAFIEAAQE QGVPGNDDYN
GATQAGAGYF QRTIDGRWRS SVANTYLKQA RGRPNLSIRT QARAQALIFG MADEPKRVTG
VAYVRAGHKA QVRARREVVV SCGALNTPRL LELSGIGDPL RLAAAGLPLR HALSGVGENL
ADHYGVRVVA RVKTATTINQ MTRGAGLLRE IGRWLLNRPN VLAVSPSIVH WFAMSAHADG
RPDLQGVFTP ASYKDGAIGV LDDFPGVTAG VWPHRPRSRG SVHVQSPDPA QPPRIEANYL
SHELDRAVLV DGIRKARAIL RGPALRPYFV EETMPGQVGD SDDELLDFAA RYGASAQHLV
GTARIGTAAD PAAVVDERLR IIGLTGVRIA DASIIPQTPS ANTCAAAMMV GERAADMIRE
DGRR
//
