ID A1D7P2_NEOFI Unreviewed; 629 AA.
AC A1D7P2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=GMC oxidoreductase, putative {ECO:0000313|EMBL:EAW21736.1};
GN ORFNames=NFIA_069070 {ECO:0000313|EMBL:EAW21736.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW21736.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW21736.1; -; Genomic_DNA.
DR RefSeq; XP_001263633.1; XM_001263632.1.
DR AlphaFoldDB; A1D7P2; -.
DR STRING; 331117.A1D7P2; -.
DR EnsemblFungi; EAW21736; EAW21736; NFIA_069070.
DR GeneID; 4590279; -.
DR KEGG; nfi:NFIA_069070; -.
DR VEuPathDB; FungiDB:NFIA_069070; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_3_1; -.
DR OMA; HGCSWWH; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000006702; 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:SF138; DEHYDROGENASE PKFF-RELATED; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..629
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012429295"
FT DOMAIN 328..342
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 565
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 609
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 610..611
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 629 AA; 67493 MW; FE02F8355F2CC178 CRC64;
MRAFYLLSLS LVAAADRPSN PNLLSYGQKG PLLGTFFGTP GADAIFDYVV VGGGNAGLTV
ASRLAQNRSA SVAVIEAGSF YEIDNGNKSI VPGYAPYFAG TDPEDYQPLI DWGFLTTPQP
GAGNRTAHYT RGKTLGGSSA RNFMLYHRPT ADSMQRWADE VGDESYTFDR MLPYFKKSCH
YTPPDQSLYV NSTNTQTPDA FEPSGGPLLV SFGNSVDAFG TWAQRAFTAV GLEEIDGLNS
GRLLGAAYGT STINPKNAQR SSSEASFLQE AIAGGSPPTI YINAMAQRIL FDENKVATGV
QVSTAGTFGT PPANYTLNAR KEVIVSAGAF QSPQLLMVSG VGACDQLSEF GIDCIHDLSG
VGQNLQDHAF FGSAHRVNVL TASASANDPS LAARQVEQYL ANATGPLSIF GAGYYGFEKL
PEPYRSQLSE TSIQALSSVP RDWPEIEWLP LNSWVGDGSN FITGDPRDGH NYATIATALG
APFSRGSVTL ADASMNTPPV IDPQWLVDPT DIDLAIQSFK RQRQIWEVLV RMGIADAREA
YPGEHVQTDS QIREYLAKSV IPVFHVAGSC KMGREDDPLA VLDNMARVFG VQSLRVVDAS
SFPFITPGHP QAVVYALAEK IADDILAGR
//
