ID Q2UJ02_ASPOR Unreviewed; 612 AA.
AC Q2UJ02;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=AO090003001409 {ECO:0000313|EMBL:BAE58463.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE58463.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE58463.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; AP007155; BAE58463.1; -; Genomic_DNA.
DR RefSeq; XP_001820465.1; XM_001820413.1.
DR AlphaFoldDB; Q2UJ02; -.
DR EnsemblFungi; BAE58463; BAE58463; AO090003001409.
DR GeneID; 5992448; -.
DR KEGG; aor:AO090003001409; -.
DR VEuPathDB; FungiDB:AO090003001409; -.
DR HOGENOM; CLU_002865_6_2_1; -.
DR OMA; KQTGFML; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000006564; Chromosome 2.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT DOMAIN 279..293
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 239
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 612 AA; 67107 MW; 23EE08448DE82A3C CRC64;
MAITEQPYDY IIVGAGVGGL VLASRLSEDA NTTVLLVEAG PNHMGDPRVE TPGLLGAMME
NPDFDWDYLT EPQVYANNRQ LGQPRGRMVG GSSALNFSLV MYPSRANFEA WESLGNDGWG
PDAMAPYLRK FHTYTPPSET TSALLSVDKY MNAENQGDQG PLPISHLDIY TPWNRAWDDT
FARLGWNNHA DPIAGRKVGS FTPPLSVDGK TGQRGYAGAY YTQDVAERKN LHLLTETMVE
RVILKKADSR VTATGIQIRT KNGQQLEVSA TREVIVSAGS LNSPQLLELS GIGAADLLQK
HNIPVVLDLP AVGENLQDHC MSTVNFEVAD PQTSADIARD PKVVQSLVEL YEKTRTGPMT
GIPVSVAYLP LVDHNGQVQR EQIDDLLAQY LDSPQVKQIS LGRQQQYKIL RQMLRDDQTG
SADYMFLVAQ FNAKEGVNTM SYALSKDLPE NYINILVLHN HPFSRGSIHI QSANAGDKPI
YDPKYLSHPL DLEILARHTQ FLDKIASTEP FSSLLKPGAR VPKAAVDLAD LDTAKEVVKD
RLFHCCHPVG TCAMMPAELG GVVDTQLKVH GTHNLRVVDA SIFPLELSGT IQATTYAVAE
RAADIIRATA HC
//
