ID A0A0G3EUG7_9BURK Unreviewed; 542 AA.
AC A0A0G3EUG7;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AKJ69669.1};
GN ORFNames=ABW99_17085 {ECO:0000313|EMBL:AKJ69669.1};
OS Pandoraea thiooxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ69669.1, ECO:0000313|Proteomes:UP000036700};
RN [1] {ECO:0000313|Proteomes:UP000036700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL Submitted (JUN-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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CP011568; AKJ69669.1; -; Genomic_DNA.
DR RefSeq; WP_047215580.1; NZ_CP014839.1.
DR AlphaFoldDB; A0A0G3EUG7; -.
DR STRING; 445709.ABW99_17085; -.
DR KEGG; ptx:ABW99_17085; -.
DR PATRIC; fig|445709.3.peg.3611; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000036700; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000036700}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 542 AA; 59190 MW; EF8C5A2596146FBF CRC64;
MPKHQGAYDY IIVGAGTAGC LLANRLTQDA DVTVLLIEAG GKDDYHWIHI PVGYLYCIGN
PRTDWLYRTQ NEAGLNGRAL AYPRGRVLGG SSSINGMIYM RGQREDYDGW AAIADDASWR
WDAVLPYFMR VEDHHKGASE FHGGGGEWRV EAQRLSWRVL DTFVEAAAQS GIPATDDFNR
GDNFGVGYFE VNQRRGVRWN ASKAFLRPAR GRPNLTILTG AQVTRLVFAG KRCVGLNYRQ
DGQECGVEAR LEVLLASGAV NSPQLLEVSG VGQGALLQQH GVAVVHDLPG VGENLQDHLQ
LRTIYRVDGV KTLNTLANHW WGKLRIGLQY ALTQGGPMSM APSQLGAFAK SDEFQARANL
QYHVQPLSLD KFGDPLHTFN AFTASVCNLR PTSRGSIHLS GPHAQQPPTI APNYLHTKED
RAVAADALRL TRRILAAPAF ARYAPREYLP GPAYQSDEEL ARAAGNIGTT IFHPVGTCRM
GRADDAGAVV DSRLRVRGLA GLRVVDASVM PTITSGNTNS PTLMIAEKAS EMIRADRIAA
RK
//
