(data stored in SCRATCH zone)

SWISSPROT: FMPF_ASPFU

ID   FMPF_ASPFU              Reviewed;         588 AA.
AC   Q4WD48;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   RecName: Full=Aromatic hydroxylase fmpF {ECO:0000303|PubMed:25582336};
DE            EC=1.14.13.- {ECO:0000305};
DE   AltName: Full=Fumipyrrole biosynthesis protein F {ECO:0000303|PubMed:25582336};
DE   AltName: Full=Monooxygenase fmpF {ECO:0000305};
GN   Name=fmpF {ECO:0000303|PubMed:25582336}; ORFNames=AFUA_6G03490;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., 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., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=25582336; DOI=10.1111/mmi.12926;
RA   Macheleidt J., Scherlach K., Neuwirth T., Schmidt-Heck W., Strassburger M.,
RA   Spraker J., Baccile J.A., Schroeder F.C., Keller N.P., Hertweck C.,
RA   Heinekamp T., Brakhage A.A.;
RT   "Transcriptome analysis of cyclic AMP-dependent protein kinase A-regulated
RT   genes reveals the production of the novel natural compound fumipyrrole by
RT   Aspergillus fumigatus.";
RL   Mol. Microbiol. 96:148-162(2015).
CC   -!- FUNCTION: Aromatic hydroxylase; part of the gene cluster that mediates
CC       the biosynthesis of fumipyrrole, a brown pigment that is involved in
CC       growth and conidiation (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P15245};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:25582336}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15245}.
CC   -!- INDUCTION: Expression is positively regulated by the fumipyrrole
CC       biosynthesis specific transcription factor fmpR (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC       {ECO:0000305}.
DR   EMBL; AAHF01000012; EAL85690.1; -; Genomic_DNA.
DR   RefSeq; XP_747728.1; XM_742635.1.
DR   SMR; Q4WD48; -.
DR   STRING; 746128.CADAFUBP00009214; -.
DR   EnsemblFungi; EAL85690; EAL85690; AFUA_6G03490.
DR   GeneID; 3505023; -.
DR   KEGG; afm:AFUA_6G03490; -.
DR   EuPathDB; FungiDB:Afu6g03490; -.
DR   HOGENOM; HOG000251017; -.
DR   InParanoid; Q4WD48; -.
DR   KO; K03380; -.
DR   OMA; NIGWKLR; -.
DR   OrthoDB; 366744at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.20; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR   InterPro; IPR038220; PHOX_C_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF07976; Phe_hydrox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q4WD48.
DR   SWISS-2DPAGE; Q4WD48.
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..588
FT                   /note="Aromatic hydroxylase fmpF"
FT                   /id="PRO_0000438874"
FT   NP_BIND         9..38
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   NP_BIND         17..18
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   NP_BIND         37..39
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   NP_BIND         45..50
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   NP_BIND         289..299
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   NP_BIND         309..313
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   BINDING         49
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   BINDING         232
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   BINDING         232
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
FT   BINDING         299
FT                   /note="FAD"
FT                   /evidence="ECO:0000250|UniProtKB:P15245"
SQ   SEQUENCE   588 AA;  65844 MW;  BEFE9CF8C3077E57 CRC64;
     MSNASDHVDV LIIGAGPAGL TTANSFNGSN CRVRLIDWKP APLETGRADG LKSISLEVLD
     SFGIGDRVLN DCQPCEEIVL WNPGKDGVIA RTMTIPDKVE ELGQIERVMV ENLYRHKTVQ
     VNWNTQPVRL HIAPVTKDEP EAHPLTITVQ NKETLGQETI RAKYVVGADG AHSWLRKYLN
     IGFSGDVTDS TWGVMNLVPK TDFPDIRKVF VVHSRAGTVM GVPREDKLVR LYISMDGGNR
     HTSIDAKSIT AENLLQAARA ILAPYRLDAA RIPWWSAYCV GQRVADEFAR HNRIFLAGDA
     VHTHSPKAGQ GMNTSIQDGY NIGWKLRYCL EQKASPALLS TYQTERRPIA QALIDFDRKY
     LESFTRRDIT HQEFLEAYLA GQRFTTGIQI QYPPSLIVTA KHLHAPSHPL ATNLAPGKRL
     PDFQMVNQSD AVPIQAYHRF TSDGRFRLLV FPGDISQALA FGRFSRLGDW LTSHLPPSSG
     LEIITIHGAR RADVELMDLH PAFRPWSDEE GWNYWTVYAD DDSYHKGHGH VYERCGISKE
     DGVLVLLRPD GYISLIASFD ETHELIDFFD GLQSGPRTVP QPERRANL
//

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