ID U4UD77_DENPD Unreviewed; 569 AA.
AC U4UD77;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN ORFNames=D910_05936 {ECO:0000313|EMBL:ERL88551.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL88551.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL88551.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KB632073; ERL88551.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UD77; -.
DR STRING; 77166.U4UD77; -.
DR Proteomes; UP000030742; 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 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742}.
FT DOMAIN 109..132
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT ACT_SITE 504
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 548
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 119..122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 569 AA; 64197 MW; B73633DEB147BD76 CRC64;
MVADFQYPTD AKQYKPVNDS IYDFGEFDFI IVGSGSTGSV IANRLTEVEN FTVLLVEAGS
YANDFVRIPG MSGDVLLLNE FNWFYRTVPQ KTICLGKRVS HLVLIFRRGK GIGGTSLLNG
LVYSRGTPES YNRIAAMGNP EWSYEQVLPY FKKLENFHKN VKNVQVENDY HGFEGLVNVE
YFPTNRHTTE LFVEAAQTIG YKSIDYNGPN FAGASVVHAV HKNGQRWDAG RAYIEPILNR
TNLNISTNSY VTKILIDPNS NRADGVQFSK DRRLYQAVAR KESGVGPKTH LQQVGIPIVH
ELEVGSTFRD QPGMYGLYFV TNYSDPNVVK GQREKLAEYV KGFGLLGTSG SDALMFASFN
QSSPQPDIEL EMTYLDPNDA YRKTFYYNNE TWNAIWNGTD GSKAFTIQTI LLFPKSTGSI
RLKSNDPYEY PLIDPKQLSD EKNIDIEKLY QGVQLALKLV DSKPFRSVDA KFINRTLPAC
AEHEYLSKDY WLCYIRHTSY ADNHFQGTNS MGPDPEKGAV VDSRCRVHGI RKLRVADASI
FPFTVANHPN APCMMVGERV SDLIKQDYL
//
