ID Q2ULQ7_ASPOR Unreviewed; 603 AA.
AC Q2ULQ7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=AO090003000309 {ECO:0000313|EMBL:BAE57508.1};
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:BAE57508.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE57508.1, 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|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; AP007155; BAE57508.1; -; Genomic_DNA.
DR RefSeq; XP_001819510.1; XM_001819458.1.
DR AlphaFoldDB; Q2ULQ7; -.
DR SMR; Q2ULQ7; -.
DR STRING; 510516.Q2ULQ7; -.
DR EnsemblFungi; BAE57508; BAE57508; AO090003000309.
DR GeneID; 5991493; -.
DR KEGG; aor:AO090003000309; -.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OMA; HVGTTWH; -.
DR OrthoDB; 2392848at2759; -.
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:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 278..292
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 537..538
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 603 AA; 65367 MW; DBE6697FF11502E0 CRC64;
MGGLYKELPE GLDEVDVIIA GGGTAGCVVA SRLSDAYPTL SILVVEGGRD NRGLQNVTYP
ILLLNNILPG NTDTLFYEGI PEKAVGNRSL VVPSGGVLGG GSSINLLTYS RAQAVDYDQW
GVEGWFSKDL VPYLQRLETY KGEGTPETHG YSGPMLVTPG NYTAKASEEG FIKAAAKLGY
PEARDIQDLE TINATQRNIR YVNGGKRQDA ASNYLHPRLG DGFHPNLHVL TQHQVIRVLF
NGNKASGVEF RPNPKFNDGV ERPVQRVSAK KLVVLSSGAL GTPLVLERSG VGDPEILGKA
GVDVVAEVPG VGAEYQDHQL MTYAYYSSLL PNETFDAIYS GRTNVDELIQ KNDPIIGWTA
ADVYSKLRPS DEEAKALGSA FESAWNRDYK TNPTKPLSMI TSLNGFPGDS TGQPEVQYFS
CSTFTPYPYS RGHLHITSKD LDASLDFATG FFADEDDIDI KKSVWSYKKQ REIIRRMDIY
RGEFAPLHPA FAADSDAATP SEPLDGPLPD DVPDIVYTAE DDAVLEQWLR AHVGTTWHSL
GTCKMAPKSE GGVVDSSLSV YGVEKLKIAD LSVPPGNVGA NTANTAYMIG EKAADIFIQE
LKA
//
