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Database: UniProt
Entry: A0A158M4M6_9BORD
LinkDB: A0A158M4M6_9BORD
Original site: A0A158M4M6_9BORD 
ID   A0A158M4M6_9BORD        Unreviewed;       552 AA.
AC   A0A158M4M6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative glucose dehydrogenase {ECO:0000313|EMBL:KAK91030.1};
GN   ORFNames=L497_2586 {ECO:0000313|EMBL:KAK91030.1};
OS   Bordetella holmesii CDC-H585-BH.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK91030.1, ECO:0000313|Proteomes:UP000026682};
RN   [1] {ECO:0000313|EMBL:KAK91030.1, ECO:0000313|Proteomes:UP000026682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK91030.1,
RC   ECO:0000313|Proteomes:UP000026682};
RA   Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C., Cassiday P.,
RA   Tondella M.L., Liao P., Zimmerman J., Meert K., Wessel D., Berger J.,
RA   Dean J.M., Holubkov R., Burr J., Liu T., Brinkac L.M., Sanka R., Kim M.,
RA   Losada L.;
RT   "Genome sequence of Bordetella holmseii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:KAK91030.1}.
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DR   EMBL; JFZZ01000065; KAK91030.1; -; Genomic_DNA.
DR   RefSeq; WP_005020171.1; NZ_JFZZ01000065.1.
DR   AlphaFoldDB; A0A158M4M6; -.
DR   STRING; 35814.BBB42_15890; -.
DR   GeneID; 56626199; -.
DR   PATRIC; fig|1331206.3.peg.1731; -.
DR   Proteomes; UP000026682; 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; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          16..57
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          246..331
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          420..540
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   552 AA;  60022 MW;  F6D8C1B998A854BA CRC64;
     MTRQAEFQAN GDAQADIVIV GSGVLGAMIA DQLAARGHAV LILEAGLRIE RGQAVENWRN
     MPFANRAGSD FQGLYPQSPD APAPLYFPEN HYVHLSGPSA GSFKQGYLRT VGGTTWHWAA
     SCWRHLPVDL RMKSTYGVGR NWPISYEQLE PFYLQAEDEM GVAGPNDPAQ QSPSERSGPY
     PMDMVPWAYG DQRFADVVNP HGYRSVPIPQ GRSIHPWRGR PTCCGNNNCQ PICPIGAMYN
     GIHHVQAAEE KGAKVLAQAV VYKIDTDENN RITAVHWYDA QRQSHKATGK HFVLACNAME
     TPRLLLMAAD ARNPKGIANR SDQVGRNLMD HSGFHCYFQS AEPLWPGRGP AQSSCLVGPR
     DGAFRARYSA NKMILNNITQ VTLATKTALA RGLSGKALDA EIRRRAAHGV DLSINLEPLP
     EPGNRVTLSK TRMDPLGLPC PDVHYDVGEY VRKGAEAAHT QLRHIGSLFG ATDFLITTDL
     NANNHMMGSV IMGSDPRDSV VDGDCRAHDH DNLWLPGGGA MPSASVVNST LSMAALGLKA
     AAAIARRLEA TS
//
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