(data stored in SCRATCH zone)

SWISSPROT: FMPE_ASPFU

ID   FMPE_ASPFU              Reviewed;        1480 AA.
AC   Q4WD47;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Nonribosomal peptide synthetase fmpE {ECO:0000303|PubMed:25582336};
DE            EC=6.3.2.- {ECO:0000305|PubMed:25582336};
DE   AltName: Full=Fumipyrrole biosynthesis protein E {ECO:0000303|PubMed:25582336};
GN   Name=fmpE {ECO:0000303|PubMed:25582336}; ORFNames=AFUA_6G03480;
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, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
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: Nonribosomal peptide synthetase; part of the gene cluster
CC       that mediates the biosynthesis of fumipyrrole, a brown pigment that is
CC       involved in growth and conidiation (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- INDUCTION: Expression is positively regulated by the fumipyrrole
CC       biosynthesis specific transcription factor fmpR (PubMed:25582336).
CC       {ECO:0000269|PubMed:25582336}.
CC   -!- DISRUPTION PHENOTYPE: Prevents the production of fumipyrrole and leads
CC       to reduced growth and sporulation, but does not affect virulence in
CC       infected mice (PubMed:25582336). {ECO:0000269|PubMed:25582336}.
CC   -!- SIMILARITY: Belongs to the NRP synthase family. {ECO:0000305}.
DR   EMBL; AAHF01000012; EAL85691.1; -; Genomic_DNA.
DR   RefSeq; XP_747729.1; XM_742636.1.
DR   SMR; Q4WD47; -.
DR   STRING; 746128.CADAFUBP00009215; -.
DR   EnsemblFungi; EAL85691; EAL85691; AFUA_6G03480.
DR   GeneID; 3505176; -.
DR   KEGG; afm:AFUA_6G03480; -.
DR   EuPathDB; FungiDB:Afu6g03480; -.
DR   HOGENOM; HOG000217009; -.
DR   InParanoid; Q4WD47; -.
DR   OMA; NGARVNW; -.
DR   OrthoDB; 58997at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; AMP-dep_Synthh-like_sf.
DR   InterPro; IPR013120; Male_sterile_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   TIGRFAMs; TIGR01746; Thioester-redct; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q4WD47.
DR   SWISS-2DPAGE; Q4WD47.
KW   Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1480
FT                   /note="Nonribosomal peptide synthetase fmpE"
FT                   /id="PRO_0000438873"
FT   DOMAIN          662..741
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          132..527
FT                   /note="Adenylation domain"
FT                   /evidence="ECO:0000255"
FT   REGION          780..1003
FT                   /note="NAD-binding domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1100..1465
FT                   /note="Aminotransferase domain"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         700
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   1480 AA;  163306 MW;  45137566A9EAC7BE CRC64;
     MLLQDVHHRE QLDDDVENAF SKINGTARQA SPFADEPSID VPSTHLPVVT PRSKTANDRT
     GLAKSLPYAS LGASRSTIDE QDVLIQTWAI LLHQYAVSDT VAFAIIGKSD PSGYSGRRAS
     TQVVCLPHLF LDSARATPHA PAVHGWDGRL TYAELDQLSN SVARQLLRRG VRKGQFVPFS
     FEKSIWMVVA IIGILRAGGV VASIDPSQPQ SRAREIIQET GATVIVASTA QASVFAGLVD
     TVVPIADDTV HPAANDTGLH PSLPPVHPED PAVVIFTSGS TGKPKGIVIQ HGAVTTRMVA
     EGRAFQYHGA RTLQFAASTW DIFMTDIFTT LAFNGCVCIP SEEDRRFNLA RFCAEYDVSL
     ALITPSLANL LEPTGFPTLK TLIFGGEALK EEVTRKWEAV DGISLHQGYG PAETGPCVAG
     RLAERPEILG YALDNSVCVL VDPSNPNRLV PLGAVGELVV GGPSLLREYI NDPRKTEAAV
     IENPPWALDL MTPVRRFYRT GDLLRYSVDT LDGRLEFVGR TDDQVKYHGQ RIELGEIEHH
     LSRLPGVEAC VVVLAKAGFF KDRLVAVVQA GKSSGGSSYG TQLSLRSDPN ITITHMRRFL
     SSRLPEFMIP NELLVVQELP HNNSMKLDRG RVAKWVADMQ SQPSEAVPKP HTRGNELLAH
     ESTARTIARE YARIVAGDSV ARRREYEDRD FNLQEGGIDS IQIMSLSMFL TEHFGFQVPM
     ADILSSRATV RSIASLIDAN SSPGRGQPLN TQETARLPLR SNGPAPSQQA LERNGSRVFL
     TGASGFLGIE ILRQLLARPK THVYALVRGS SESQARERLV QKAISAGWWQ DAYRTRLHVW
     HGDLTQPQLG LSQLQWQMLQ GKASPSIDAI IHNGAKVHYS QDYETLKKTN VSPTVELLKA
     VHDREEPLHS FVFVSGGQQL SFDDREDEKN AAKSLKGSGY ARSKAVSEQI VRRFANQKGS
     KARHVRIVKP GFIIGDAERG LANQSDFIWR LIAACVELGF YNGDEADSWL FISDITRVAQ
     VILHSVFEDD SQPVTKVLDG LRFKTLWALL QDKFGFELQP LSRREWLARL KHSVATKKEK
     HVLLREQFPA LHHGVVPFNN AAGTVVHREA AESTHRYMTS FPYELGRDDP ASAAKTQRLQ
     DRFAELAAFM NADPDEIAFG QSTTFLLRSL GQALKPLLNS DCEIIVSILC HEGSAAAWVA
     LAKDLGIAIK WWAPPPGDDP VLSLDTLRPL LTPKTRLVAC NHVSNVVGTI HPIRQVADLV
     HRIPGAVLVV DGVAWAPHRP IDVKALDVDF YCFSWYKVFG PHVAQLYGRR SAQKRALAGI
     SHFFLSEMPG LDWRLRLGAN SFELEEALVP ITRYLKRVGW DNIIAQETVL QDVFLAYLRR
     RPRVFRIFGE QSSDPAKRVP VITFEVIGHS STVVANKVNQ RGRFRVVSGN CWAPRPTHDV
     LGLGADGLIR VSFVHYNTVA EVQEFCTELD SVLETLNAGI
//

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