ID   A0A443SDL6_9ACAR        Unreviewed;       399 AA.
AC   A0A443SDL6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN   ORFNames=B4U80_11265 {ECO:0000313|EMBL:RWS25608.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS25608.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS25608.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS25608.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
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:RWS25608.1}.
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DR   EMBL; NCKV01003532; RWS25608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443SDL6; -.
DR   STRING; 299467.A0A443SDL6; -.
DR   EnsemblMetazoa; LDEU006432-RA; LDEU006432-PA; LDEU006432.
DR   VEuPathDB; VectorBase:LDEU006432; -.
DR   Proteomes; UP000288716; 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; PS00623; GMC_OXRED_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288716}.
FT   DOMAIN          117..140
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
SQ   SEQUENCE   399 AA;  44181 MW;  30B176E5FDB16F66 CRC64;
     MVDLVPTIPA LVPLLALIYV RSSDHSFSVT RNNWDLEYDF IIVGGGSSGA VMANRLTENP
     NWKVLLLEAG GSDNILSDIP LAAANLQGTP LDWAYQTEPQ EAACYGLNNR RMKWPRGRVL
     GGSSVLNYML YVRGNRRDFD NWVRLGCEGW SFEEVFPYFI KSEDNQDPSI AFNGWHGVGG
     YLTVSTPPDP TPLGTAFPEA GKFLGYANID LNGPMQTGFA IPQGTIRRGA RCSTSKAFLL
     PAKDRPNLHY LTTGRGPLTI LGGVEGLGFI KTKYANYSDD FPDFQVHLLS GIDTFSLYPV
     LLQPKSRGLI KLRSTSPYDP PIIDPKYLTH PDDIMAMVDA MKICIAIGLT PAYRKFGTQL
     FERVMPGCES YAMLSDEYLA CMARTYTQTI YHPTFIGIT
//