ID A0A0G3BXR8_9BURK Unreviewed; 558 AA.
AC A0A0G3BXR8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AKJ32191.1};
GN ORFNames=AAW51_5500 {ECO:0000313|EMBL:AKJ32191.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ32191.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ32191.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ32191.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-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}.
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DR EMBL; CP011371; AKJ32191.1; -; Genomic_DNA.
DR RefSeq; WP_047197151.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BXR8; -.
DR STRING; 413882.AAW51_5500; -.
DR KEGG; pbh:AAW51_5500; -.
DR PATRIC; fig|413882.6.peg.5750; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000035352; 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:UP000035352}.
FT DOMAIN 277..291
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 558 AA; 62129 MW; F9161752898F643F CRC64;
MPSSSTSDSF DYVIIGAGTA GCLLANRLSR DGRHRVLLLE AGRRDDYHWI HIPVGYLYCI
GNPRTDWLYH TEAEPGLNGR QLRYPRGKGL GGCSSINGMI YMRGQRRDYD GWAALCRDDS
WRWDACLPYF KQHENHWRLD PLHADQASDA FKAAHGHGGE WRVERQRLRW DVLDAFALAA
QQAGVPASDD FNRGDNEGVG YFEVNQRAGW RWNTAKAFLR PVCLTRPNFV LCTGAHVTRL
STERDADGVL RATGCEVVTR EGRRTVTATR EVILAAGAIG TPQLLQLSGI GPADWLHRHG
IAVQHDLPGV GENLQDHLQI RAVYAVQGVK TLNTLARSWW GKAMIGLEYA WRRSGPMSMA
PSQLGAFTRS SPEQPWPNLE YHVQPLSLDA FGEPLHRFNA FTASVCNLNP SSRGHVRVHS
PRFEDAPQIR PCYLSTEADR QVAADSLRMT RRIVSQPALQ RFRPEEVKPG VQYQSDEELA
TLAGDIATTI FHPVGTCRMG RPDDPMAVVD PRLRVRGVRG LRVVDASVMP TITSGNTNSP
TLMMAERAAE WILAASTG
//
