ID A0A142LKM6_9PROT Unreviewed; 535 AA.
AC A0A142LKM6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:AMS32772.1};
GN ORFNames=AEM42_10980 {ECO:0000313|EMBL:AMS32772.1};
OS Betaproteobacteria bacterium UKL13-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1690485 {ECO:0000313|EMBL:AMS32772.1, ECO:0000313|Proteomes:UP000075227};
RN [1] {ECO:0000313|Proteomes:UP000075227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Driscoll C.B.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012157; AMS32772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142LKM6; -.
DR STRING; 1690485.AEM42_10980; -.
DR KEGG; beb:AEM42_10980; -.
DR PATRIC; fig|1690485.4.peg.2500; -.
DR Proteomes; UP000075227; 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; PS00623; GMC_OXRED_1; 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 ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000075227}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 255..269
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 535 AA; 57734 MW; 6614E622C9198307 CRC64;
MSDCITDYLI LGAGSAGCTL AGRLSERSDT HVTLLEAGPR DSSVLIHCPA GMAVMAQTGT
ANWGFNTVPQ RGLYGRKGYQ PRGKVLGGSS SINAMIYARG HRADYDHWAE LGNTGWAYQD
VLPYFKRAEN NERGSDRFHG VGGPLNVRDL ASPNRYSQAF IDAGHEAGFP INHDFNGAEQ
EGVGLYQVTH RAGERFSAAK AYLAPNRGRS NLTIETNAQV TRILFEGRRA VGAEFVQNGT
LRQIRVRREV LLSAGALQSP QILMLSGVGS ADALSKLGIP VVHHLPGVGL NLHDHADAVQ
VYDAPKLTDL LGVSVTGVWH LLKGIAEWRS HRTGLLTTNI AEAGGFVRSS PAEAIPDLQF
HFVIGKLVDH GRKVTFGHGY SCHVCVLRPK SRGSVTLQSS DPLAAPLIDP NFLDDPEDMA
RMVKGFRIMR DVLAQPALSR YGGRELNRSA TAQTDAEIEG FIRSQADSIY HPVGTCRMGG
DDAAVVDASL RVHGIEALRV IDASVMPRIV GGNTNAPTIM IAEKAADMIR QNIKL
//
