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Database: UniProt
Entry: A0A182H3F9_AEDAL
LinkDB: A0A182H3F9_AEDAL
Original site: A0A182H3F9_AEDAL 
ID   A0A182H3F9_AEDAL        Unreviewed;       628 AA.
AC   A0A182H3F9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=RP20_CCG020917 {ECO:0000313|EMBL:KXJ81243.1};
OS   Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF020917-PA.1, ECO:0000313|Proteomes:UP000069940};
RN   [1] {ECO:0000313|EMBL:KXJ81243.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ81243.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ81243.1};
RX   PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA   Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA   Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA   Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA   Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA   Yan G., Tu Z.J., Fang X., James A.A.;
RT   "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT   insights into its biology, genetics, and evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN   [2] {ECO:0000313|EMBL:KXJ81243.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ81243.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ81243.1};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:AALF020917-PA.1}
RP   IDENTIFICATION.
RC   STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF020917-PA.1};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
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; JXUM01024565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KQ560694; KXJ81243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182H3F9; -.
DR   STRING; 7160.A0A182H3F9; -.
DR   EnsemblMetazoa; AALF020917-RA; AALF020917-PA; AALF020917.
DR   VEuPathDB; VectorBase:AALC636_011825; -.
DR   VEuPathDB; VectorBase:AALF020917; -.
DR   VEuPathDB; VectorBase:AALFPA_056670; -.
DR   Proteomes; UP000069940; Unplaced.
DR   Proteomes; UP000249989; 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:SF208; 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.
DR   PROSITE; PS00624; GMC_OXRED_2; 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:UP000249989}.
FT   DOMAIN          143..166
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          320..334
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   628 AA;  69284 MW;  02D173326D2155D1 CRC64;
     MALSVKLCVL AIAIGILCIG SGDAFFFLLK SLAHIGRYDD GYDDQYNYVQ PTYGNPQVKE
     IPEYDFIIVG AGPAGCVLAN RLSENSRWKV LLLEAGPGEN ELNNIPILTT FLQNSQYNWA
     DVAEAQNDSC WGMIDQRCSI PHGKGLGGST LINYMMYTRG NPADYDRWAS MGNPGWSYSD
     VYPYFLKTER ASLRGLENSS YHGYDGELSV EFPPFRTDLA RTFVKGAREI GHKKIDYNGK
     GQLGVSYVQT NTINGMRQTA YRALIQPILA NRPNLHVKAY SRVIKVLINP NTKSAYGVTY
     TKNFRNFDIH ARKEVIVTAG AINTPQLLML SGVGPEDTLQ DIKVPVVQNL PVGQNMIDSI
     VFNGLTFVLN ETGHALLTDS RFQLNSIADY FNGQGPLTVP GGVEAVDFLQ TSRAEQPGVP
     DIAVIFSTGS LVSDGGLGLR SGKRIKTSLY NKVYKPLETL PNDQWTATVS LLHPKSRGFI
     KLRNANPFNS PKIYTNYLTE DNDVETLLEG IKEAVRLSKS PSMKRYDARV LGIPLPNCKQ
     YEISSDDYWR CAIRTLSSTA YQQLGTCKMG PHGDPTAVVS AELEVHGVEN LRVADVSVVP
     TTISGHSAAI DYMIGEKAAD LIKQRWAM
//
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