ID L0IVB8_9MYCO Unreviewed; 652 AA.
AC L0IVB8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Choline dehydrogenase-like flavoprotein {ECO:0000313|EMBL:AGB23019.1};
GN ORFNames=Mycsm_02690 {ECO:0000313|EMBL:AGB23019.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB23019.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; CP003078; AGB23019.1; -; Genomic_DNA.
DR AlphaFoldDB; L0IVB8; -.
DR STRING; 212767.Mycsm_02690; -.
DR KEGG; msa:Mycsm_02690; -.
DR PATRIC; fig|710686.3.peg.2707; -.
DR HOGENOM; CLU_002865_4_1_11; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000010844; 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:SF213; DEHYDROGENASE, PUTATIVE-RELATED; 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; 2.
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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT DOMAIN 340..354
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 652 AA; 72804 MW; 871DDB31EDE9531A CRC64;
MTASGHHDSF DYIVVGSGAG GGPLAARLAE AGMRVLLLEA GAEGLADHDS DDYAVPAFHG
RATEDPATSW QYFVRHYANR KQQERDSKFV AARDGVFYPR AAALGGCTAH NAMITIYPHA
EDWNEIYELT GDESWRAENM RTYFERLEDC GYRWRPWRLP ANRLLAALAT HLPLLNHRFR
NDARHGFGGW LHTALADPLM ALEDKKICAL LGDAAQANVA EFWQRRGDLF AGPRSWLDPN
DWRLRDSPDG VWEIPMAVQR GRRNGSRERI RDVARRLPHR LVVRTGCLVT RVLLDEEPAA
TGVEYIHAPH AYWCDPCPAR GPMPPVQTAC ATQEVILAAG AFNSPQLLKL SGIGAAAELG
PLGIEPRVEL PGVGRNLRDR YEVAVVSRMT RDFSLLSRRN RFRPPFPGER PDPAYRRWRW
CGKGVYATNG TVVGVVRRSD YGRAAPDLFV FGLPARFEGY YPGYSCELEH HRDYFTWAIL
KAHTENRAGE VRLRSADPRD PPVIDFHYFE EGSDTKGEDL DAVVKGVRIA RDIMSRAGTA
VAEEVSPGPE VQTDDQLKEW IRDNAWGHHA SCTCPIGKRA DGAVTDGSFR VHGVGRLRVV
DASVFPRIPG FFIVTSIYML AEKASETILA DAAKHLTGNP TRLIHARHCR PR
//
