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Database: UniProt
Entry: Q4WFN7_ASPFU
LinkDB: Q4WFN7_ASPFU
Original site: Q4WFN7_ASPFU 
ID   Q4WFN7_ASPFU            Unreviewed;       646 AA.
AC   Q4WFN7;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   10-APR-2019, entry version 82.
DE   SubName: Full=GMC oxidoreductase, putative {ECO:0000313|EMBL:EAL86440.1};
GN   ORFNames=AFUA_3G01580 {ECO:0000313|EMBL:EAL86440.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL86440.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL86440.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M., Fedorova N., Fedorova N., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.,
RA   Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafon A., Latge J.P., Li W., Lord A., Lu C.,
RA   Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M.,
RA   Mouyna I., Mulligan S., Murphy L., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J., Yu J.H., Fraser C., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAL86440.1}.
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DR   EMBL; AAHF01000010; EAL86440.1; -; Genomic_DNA.
DR   RefSeq; XP_748478.1; XM_743385.1.
DR   STRING; 746128.CADAFUBP00004591; -.
DR   EnsemblFungi; EAL86440; EAL86440; AFUA_3G01580.
DR   GeneID; 3505842; -.
DR   KEGG; afm:AFUA_3G01580; -.
DR   EuPathDB; FungiDB:Afu3g01580; -.
DR   HOGENOM; HOG000139601; -.
DR   InParanoid; Q4WFN7; -.
DR   OMA; NEGVGYF; -.
DR   OrthoDB; 798314at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
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; -; 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   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002530};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT   DOMAIN      284    298       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND      37     38       FAD. {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   ACT_SITE    529    529       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000137-1}.
FT   ACT_SITE    573    573       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000137-1}.
FT   BINDING     244    244       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000137-
FT                                2}.
SQ   SEQUENCE   646 AA;  72151 MW;  CF4C6CB63AC5565C CRC64;
     MKLQVDLDPL LKLGDQTSKT DRSAAWVRLA TRKIGGTSGC VVAGRLAENP DIKILVIEAG
     QHNRELENVH MAGGWSNNFD SETDWNLITK PMPGVDNRQV KLSRGRFLGG SSGCNGTLCI
     RGAKQDYDDW ELEGWSGEEF FAAMRKAETF HTKPWFKADE NSHGYSGPLH TEPHDLAPIA
     NLLMDSFVSQ GLPLHHDMFS TGDIPHGCGH VPRTVYKGIR TTAADYITKE YHRNNGTIQT
     DTTVDRVVLE QGPDGLRATS VITQLADGTP RTFHARKEII VSGGAYCSPA ILMRSGIGAR
     AELDQHGIPC QVDLPGVGKN LLDHLIVFMF YETEKEGLTN DFHVYHDNNF AKTYQQWKEH
     KSGFLSTFPF GCFAFARLDD RLKDEPLWRD APRQPGRDPM GLTPKQPNIE FFTTECYGGP
     KQYNQFPVDK KHAFSMIAEL FAPKSRGTVT LKSKDPKENP VIDCNYLSDP LDLLVLTEAC
     RFGNEIVMNG AGTKDIVKGS WPPNLKHHTY KTREEWIPYV KEHATTCYHA AGTCAMGKDG
     DSMAVLDNKL RVRGVAGLRV ADCSVMPTLH GGHTQMPAYG IGERCADFIK ETCFRFFAKK
     EVNCCRIEKK LDDLQSHALP LSYQSWSGQS GKYCAISFKN REQRKL
//
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