ID   A0A0T6BG45_9SCAR        Unreviewed;       228 AA.
AC   A0A0T6BG45;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
DE   Flags: Fragment;
GN   ORFNames=AMK59_2218 {ECO:0000313|EMBL:KRT86155.1};
OS   Oryctes borbonicus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC   Scarabaeidae; Dynastinae; Oryctes.
OX   NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT86155.1, ECO:0000313|Proteomes:UP000051574};
RN   [1] {ECO:0000313|EMBL:KRT86155.1, ECO:0000313|Proteomes:UP000051574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OB123 {ECO:0000313|EMBL:KRT86155.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KRT86155.1};
RA   Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA   Roedelsperger C.;
RT   "Draft genome of the scarab beetle Oryctes borbonicus.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:KRT86155.1}.
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; LJIG01000785; KRT86155.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T6BG45; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000051574; 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:SF227; GLUCOSE DEHYDROGENASE [FAD, QUINONE]-LIKE PROTEIN; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000051574}.
FT   DOMAIN          18..32
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRT86155.1"
FT   NON_TER         228
FT                   /evidence="ECO:0000313|EMBL:KRT86155.1"
SQ   SEQUENCE   228 AA;  25517 MW;  86127CD2B6CBE145 CRC64;
     LVHHYYMNTI KEVILSAGSI NSPQILMLSG IGPKEELEKF QIPVIQNLKV GENMQDHVAL
     GGLTFVIDEP ISLRLERVSG IRTVMNYAAM GDGPLTVLGG VEGLAFVNTK YANKSEDFPD
     IEFHFVSGST NSDASQLSKV HGLTHEFYNR TFGPITAEDT WSVIPMLLRP RSRGVVKLKS
     KNPFHYPLIY ANYFQDNHDM KVLVEGVKIA MALSKTRPFR KLKSYFNG
//