ID A0A0G3IRQ3_9MYCO Unreviewed; 532 AA.
AC A0A0G3IRQ3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:AKK30405.1};
GN ORFNames=AB431_10025 {ECO:0000313|EMBL:AKK30405.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK30405.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK30405.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK30405.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP011773; AKK30405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3IRQ3; -.
DR STRING; 1545728.AB431_10025; -.
DR KEGG; mye:AB431_10025; -.
DR PATRIC; fig|1545728.4.peg.2043; -.
DR Proteomes; UP000035237; 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; 2.
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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT DOMAIN 96..315
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 405..521
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 464
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 499
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 532 AA; 58307 MW; 3BC0ABD131688D96 CRC64;
MVPNNGFRTN HRLRADMREF GPDDEVDVVI VGAGAGGATL GQRLARAGWR VVLLDAGPFW
DPDRDWVSDE RGSHGLYWTD PRQIGGSNPV PMGSNNSGRG VGGSMVHYAG YTPRFHPSDF
RTYTSDGVGV DWPIEYADLR PYYEQIEAEL PVAGQDWPWG DPHRYPHSPH PVSGNGLIAL
RGARALGVDM RVGPVAIPNG RFGNRPHCIY RGFCIQGCKV NAKASPLITH IPDALAHGAE
VRPDCHVSRV LVDDDTGRAT GVLYFRDGKV HRQFARSVVI AGYSIETPRL LLLSATARYP
DGLGNDHDHV GRHLMVQGAP QVAGRFDEEI RMYKAPPPEV SSEQFYETDP SKPYRRGFSI
QTVSPLPITW SEHVAAQGHW GQTLREYMRD YVHWSTLGAL CELLPLPDNR VTLADETDRH
GLPVAHFAYS QCDNDKQLID AAGTVMADLL RAAGAEEVMS VERYAHLVGG ARMATRPQDG
VIDAEHRVFG VARLYVVDGS VMPTQGAANP ALTVMALAAR AAELMKRHAV AS
//
