ID B2HEX5_MYCMM Unreviewed; 561 AA.
AC B2HEX5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Dehydrogenase fad flavoprotein Gmc oxidoreductase {ECO:0000313|EMBL:ACC41393.1};
GN OrderedLocusNames=MMAR_2954 {ECO:0000313|EMBL:ACC41393.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41393.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC41393.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
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; CP000854; ACC41393.1; -; Genomic_DNA.
DR RefSeq; WP_012394649.1; NC_010612.1.
DR AlphaFoldDB; B2HEX5; -.
DR STRING; 216594.MMAR_2954; -.
DR KEGG; mmi:MMAR_2954; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_11; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000001190; 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:UP000001190}.
FT DOMAIN 278..292
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 561 AA; 61186 MW; DFB76B389C4C5B02 CRC64;
MSPVAEFDFI IVGAGSAGCL LANRLSANPD HRVLVIEAGG KDNWFWIKVP VGYLYTIANP
RTDWCFTTEA DPGLAGRSIH YARGRVIGGC SSINAMIHMR GQASDYDLWA QATGDQRWLW
GGPDSSGETL AIYKKLENYF GGADDWHGAG GEIRVERPRV HWKILDAWQA AAAQVGIAPI
DEFNRGDNAG SAYFHVNQRR GRRWSMADAF LHPVAHRPNL TIYTQTQALK LLVDNQVRED
QRRGAWATAQ HRATGVRLLK DGQIVDVRAR REVILSAGAI GSPQLMQASG LGPAGLLAEH
QVPVAVDLPG VGENLQDHLQ LRTIYRVRGA RTVNTLYRNW ISRAGMGLQY LLLRSGPLTM
PPSTLGAFAK SDPALASPDL EWHVQPLSLP KFGEPLHRFG AITPSVCNLR PSSRGHVRIT
SGDPLTKPKI LCNYLSTDQD RQLAVRGLRM TRQIMAAPSL ARYCPEELLP GPQLVSDEDL
QKAARELGTT IFHPVGTCAM GAFDARGRPR SAATVLDTDC RVYRVAGLRV ADASAMPTIT
SGNTNAPVML VAERAARAIL G
//
