ID A0A0S8DEM3_9PROT Unreviewed; 528 AA.
AC A0A0S8DEM3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=AMJ66_05115 {ECO:0000313|EMBL:KPK33691.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK33691.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK33691.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK33691.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK33691.1}.
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DR EMBL; LJTS01000067; KPK33691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DEM3; -.
DR PATRIC; fig|1703389.3.peg.2650; -.
DR Proteomes; UP000051602; 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; 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}.
FT DOMAIN 79..102
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 251..265
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 81
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 216
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 528 AA; 57240 MW; BA49AE6BAFA7ACC8 CRC64;
MQPDYIVVGA GTAGSLLAAR LAESNANVLL LEAGPEARHP MIHIPAGVRS LHRNPALNWT
YFTEPHPDTA NRAIHWPRGR VIGGSGSING MLYVRGNPGD YDDWSDMGCS GWSYADVLPY
FRKTERYESG DPHYRGKDGP LNVVDYKSHL NLTHRFVQAA QQAGLPFNRD YNGEQQEGVA
YSQMTRLGRF RGSTAFALLR PARSRPNLQV TTNAFVTKLV FEGRQCVGAT FRKSGQDTTV
RARREVILCG GAINSPHLLM LSGIGPGTEL QSLGIPVLHD APGVGKNLID HYYGGISARV
RNELSINQLA RGWRLGREVL RFLVMGEGAL TYGITASTVF TRSRPELARP DLQLLFTPAS
YNRERFGELE AAPGVTAVVC IVQPQSRGAL TLQSADPNLP PRIEPNYLTA ANDVHALLAG
VHLVRRIFTA PAMAKCMVGE TYPGPQANTD EAIVDALRLT GTTGYHAVGT CRMGSDAEAV
VDPQLRVNGV ERLRVVDASI MPMVPTGNTN APTAMVAEKA ADLIRASA
//
