ID G7XVN0_ASPKW Unreviewed; 847 AA.
AC G7XVN0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:GAA90989.1};
GN ORFNames=AKAW_09103 {ECO:0000313|EMBL:GAA90989.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA90989.1};
RN [1] {ECO:0000313|EMBL:GAA90989.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA90989.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; DF126477; GAA90989.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XVN0; -.
DR STRING; 1033177.G7XVN0; -.
DR VEuPathDB; FungiDB:AKAW_09103; -.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; G7XVN0; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR049326; Rhodopsin_dom_fungi.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF123; GMC OXIDOREDUCTASE (AFU_ORTHOLOGUE AFUA_2G01770)-RELATED; 1.
DR Pfam; PF20684; Fung_rhodopsin; 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.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 379..402
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 554..568
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 847 AA; 92745 MW; 412B34CE7A93B00C CRC64;
MGSITEAIGK RTAELSHDGR DVAITLAVCV FLATLITGLR FWLSRRRRPL FSMPESMTLV
SLLLFYSYAV ATYLILTIGH GGYPTSQTQS WRLTFTLKCV YYLRLAYATG LGLVKCSILM
ALFRSLAASS KAARHAILVI MAVCISWSLG ATLISLLNCR PLSYNWNLQQ SEGHCINRNA
AFMAVSIIDV VTNAAILVLP LPRIIRTKIT LPEKLVMISL LILGLFVVAI TAVRTVTIAR
MDFSAINDHG KMISIWTTVE WTVALMIANS PVLWPLLDWL APFHSMENAP VDTNMTTSEQ
FDYIIVGGGT AGCVLASRLK QYNSSLSILL IEAGPDASNH PLVPDGSKAT QLLGSELDWT
YETVPQKHLS DRVLSNHAGK ALGGSTTINS GGWMRGTKED YDLWASLVGD SRWSYQGLLP
YFRKLEHHFD PSADPEVHGF GGSIKTESVS STGRRYPLRQ MVQEAWNSVG VKYNPDINSG
SPFGLADVVE NRENGMRQMS SSVYTLDVEI MTETLVKRVL VEERGSQKVA IGVVLEDKDE
SQIMARQEVI IAAGAYRTPQ LMMLSGIGPA EELRAYGINV VLDLPDVGRH FADHVAVSQW
WQLKHPENGL AFGSPAFTDP AFFRGNPIDF VALDSVPLDG LRQALVKDDP NCNPDEHPLI
TSQRVHVETF TVYVAHNAQD PSIAVDGTHI TTGVSCMLPT SRGSINLADR DVRSAPRIDP
NYCATEADRY VLREGLRKLR EVLCDTPAGQ KMILSETVEE KYQPLGPDTG DEAIDDLIRR
RAATLYHPTG GACMGKVVDG DLRVKGIDGL RVVDASVIPT PLSTHIQACV YALAEQAADI
ISGVCSV
//
