ID ENCC_ASPFU Reviewed; 181 AA.
AC A4DA85;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Anthrone oxygenase encC {ECO:0000303|PubMed:22492455};
DE EC=1.-.-.- {ECO:0000305|PubMed:22492455};
DE AltName: Full=Endocrocin synthesis protein C {ECO:0000303|PubMed:22492455};
GN Name=encC {ECO:0000303|PubMed:22492455}; ORFNames=AFUA_4G00225;
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293;
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 BIOTECHNOLOGY.
RX PubMed=20379952; DOI=10.1055/s-0030-1249779;
RA Gautam R., Karkhile K.V., Bhutani K.K., Jachak S.M.;
RT "Anti-inflammatory, cyclooxygenase (COX)-2, COX-1 inhibitory, and free
RT radical scavenging effects of Rumex nepalensis.";
RL Planta Med. 76:1564-1569(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22492455; DOI=10.1128/aem.07710-11;
RA Lim F.Y., Hou Y., Chen Y., Oh J.H., Lee I., Bugni T.S., Keller N.P.;
RT "Genome-based cluster deletion reveals an endocrocin biosynthetic pathway
RT in Aspergillus fumigatus.";
RL Appl. Environ. Microbiol. 78:4117-4125(2012).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23592999; DOI=10.1371/journal.ppat.1003289;
RA Berthier E., Lim F.Y., Deng Q., Guo C.J., Kontoyiannis D.P., Wang C.C.,
RA Rindy J., Beebe D.J., Huttenlocher A., Keller N.P.;
RT "Low-volume toolbox for the discovery of immunosuppressive fungal secondary
RT metabolites.";
RL PLoS Pathog. 9:E1003289-E1003289(2013).
RN [5]
RP INDUCTION.
RX PubMed=26242966; DOI=10.1111/1462-2920.13007;
RA Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
RT "Redundant synthesis of a conidial polyketide by two distinct secondary
RT metabolite clusters in Aspergillus fumigatus.";
RL Environ. Microbiol. 18:246-259(2016).
CC -!- FUNCTION: Anthrone oxygenase; part of the gene cluster that mediates
CC the biosynthesis of endocrocin, a simple anthraquinone interesting for
CC many biotechnological applications (PubMed:22492455, PubMed:23592999).
CC The pathway begins with the synthesis of atrochrysone thioester by the
CC polyketide synthase (PKS) encA (PubMed:22492455). The atrochrysone
CC carboxyl ACP thioesterase encB then breaks the thioester bond and
CC releases the atrochrysone carboxylic acid from encA (PubMed:22492455).
CC The atrochrysone carboxylic acid is then converted to endocrocin
CC anthrone which is further oxidized into endocrocin by the anthrone
CC oxygenase encC (PubMed:22492455). The exact function of encD has not
CC been identified yet, but it negatively regulates endocrocin production,
CC likely through the modification of endocrocin itself (PubMed:22492455).
CC {ECO:0000269|PubMed:22492455, ECO:0000269|PubMed:23592999}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Endocrocin is specifically produced in conidia.
CC {ECO:0000305|PubMed:23592999}.
CC -!- INDUCTION: Expression is positively regulated by the transcription
CC factors brlA and laeA (PubMed:26242966). {ECO:0000269|PubMed:26242966}.
CC -!- DISRUPTION PHENOTYPE: Leads to unstable anthrone production and
CC abolishes the production of endocrocin (PubMed:22492455).
CC {ECO:0000269|PubMed:22492455}.
CC -!- BIOTECHNOLOGY: Endocrocin and related anthraquinones compounds have
CC interesting activities for medicinal uses, including anti-inflammatory
CC activity (PubMed:20379952). {ECO:0000269|PubMed:20379952}.
CC -!- SIMILARITY: Belongs to the anthrone oxygenase family. {ECO:0000305}.
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DR EMBL; AAHF01000017; EBA27176.1; -; Genomic_DNA.
DR RefSeq; XP_001481526.1; XM_001481476.1.
DR AlphaFoldDB; A4DA85; -.
DR STRING; 330879.A4DA85; -.
DR EnsemblFungi; EBA27176; EBA27176; AFUA_4G00225.
DR GeneID; 5077074; -.
DR KEGG; afm:AFUA_4G00225; -.
DR VEuPathDB; FungiDB:Afu4g00225; -.
DR eggNOG; ENOG502SBMN; Eukaryota.
DR HOGENOM; CLU_105974_1_0_1; -.
DR InParanoid; A4DA85; -.
DR OMA; LAWCASD; -.
DR OrthoDB; 1561590at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:1900602; P:endocrocin biosynthetic process; IMP:AspGD.
DR InterPro; IPR013901; Anthrone_oxy.
DR PANTHER; PTHR35042; ANTHRONE OXYGENASE ENCC; 1.
DR PANTHER; PTHR35042:SF1; DUF1772-DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08592; Anthrone_oxy; 1.
PE 1: Evidence at protein level;
KW Membrane; Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..181
FT /note="Anthrone oxygenase encC"
FT /id="PRO_0000437095"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 181 AA; 19473 MW; D69FD4D3CB2FA797 CRC64;
MASVQGLIKI VAITGGVWLS GKITAHSLVS VPALLQTRSA DGLSPCTILR VWRRIYEQGH
RHSPQIAACT STAFAYLAWC ASDRTPRLLY GTAACSVMGI VPYTLLFMGP TNSRLLERSA
AEEEKVPGAT RGEDMVNVPS EMTTEELLSH WRFLAGIRGL LPLAGGILGL FAALYSNEGA
R
//
