ID K0URS1_MYCVA Unreviewed; 533 AA.
AC K0URS1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EJZ05313.1};
GN ORFNames=MVAC_25675 {ECO:0000313|EMBL:EJZ05313.1};
OS Mycolicibacterium vaccae ATCC 25954.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ05313.1, ECO:0000313|Proteomes:UP000006072};
RN [1] {ECO:0000313|EMBL:EJZ05313.1, ECO:0000313|Proteomes:UP000006072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ05313.1,
RC ECO:0000313|Proteomes:UP000006072};
RX PubMed=23105074; DOI=10.1128/JB.01462-12;
RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL J. Bacteriol. 194:6339-6340(2012).
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, ECO:0000256|RuleBase:RU003968}.
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:EJZ05313.1}.
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DR EMBL; ALQA01000083; EJZ05313.1; -; Genomic_DNA.
DR RefSeq; WP_003931881.1; NZ_JH814694.1.
DR AlphaFoldDB; K0URS1; -.
DR PATRIC; fig|1194972.3.peg.5112; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_11; -.
DR Proteomes; UP000006072; 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; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968}.
FT DOMAIN 80..103
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 90..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 533 AA; 57529 MW; 47C44887E65799F7 CRC64;
MTRYDYIIAG AGSAGCVLAN RLSADPKVNV LLLEAGGGDR NLWLHIPKGS GKLFDSDRHM
WHYETTPFGP NPHVEQWMRG KVIGGSSSIN GMVYNRGQRA DYDGLEALGN KGWGWDDILP
IFTAFEDNEF GASATRGVGG PLHISVPRDP DPLCEEMIEA AAGTGLWRVQ DINESDGERV
GYATSTIRNG RRVSAATAFL KPALSRPNLT LRTGAVVRRV VFDGDRATGV EVAAGSGTEE
LQAAREVILA LGSLNSPKAL QLSGIGPREV LTAAGVAVRL DRENVGRRMR EHRCATLRLR
LKEDLGYNRR LATSFGQALT GMKYLATRKG PLAAPSFDIV GFVKTQPDAE RPDAQIMMGP
WTLPPYNTGE PVVIEREPGI SCLGMVLRPT SQGYVEITSS DPAGALRINP NYLTTAHDRE
ATANLMRRMR SVFEQSPIAE RISHETYPGP QVHSDEQLVD TALDGGYCGY HAVGTCAMGP
DEDDVVDSQL RVRGVEGLRV VDCSVMPTMV AGNLNGPVMA MAGRASEFIR GGS
//
