ENCD_ASPFU
ID ENCD_ASPFU Reviewed; 337 AA.
AC Q4W946;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=2-oxoglutarate-Fe(II) type oxidoreductase {ECO:0000303|PubMed:22492455};
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=Endocrocin synthesis protein D {ECO:0000303|PubMed:22492455};
GN Name=encD {ECO:0000303|PubMed:22492455}; ORFNames=AFUA_4G00230;
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;
OC Aspergillus subgen. Fumigati.
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 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: 2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene
CC cluster that mediates the biosynthesis of endocrocin, a simple
CC anthraquinone interesting for many biotechnological applications
CC (PubMed:22492455). The pathway begins with the synthesis of
CC atrochrysone thioester by the polyketide synthase (PKS) encA
CC (PubMed:22492455). The atrochrysone carboxyl ACP thioesterase encB then
CC breaks the thioester bond and releases the atrochrysone carboxylic acid
CC from encA (PubMed:22492455). The atrochrysone carboxylic acid is then
CC converted to endocrocin anthrone which is further oxidized into
CC endocrocin by encC (PubMed:22492455). The exact function of encD has
CC not been identified yet, but it negatively regulates endocrocin
CC production, likely through the modification of endocrocin itself
CC (PubMed:22492455). {ECO:0000269|PubMed:22492455}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22492455}.
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: Results in increased endocrocin production
CC (PubMed:22492455). {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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AAHF01000017; EAL84395.2; -; Genomic_DNA.
DR RefSeq; XP_746433.2; XM_741340.2.
DR AlphaFoldDB; Q4W946; -.
DR SMR; Q4W946; -.
DR STRING; 746128.CADAFUBP00009783; -.
DR EnsemblFungi; EAL84395; EAL84395; AFUA_4G00230.
DR GeneID; 3503737; -.
DR KEGG; afm:AFUA_4G00230; -.
DR VEuPathDB; FungiDB:Afu4g00230; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_3_1; -.
DR InParanoid; Q4W946; -.
DR OMA; KYAMAPG; -.
DR OrthoDB; 755305at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1900602; P:endocrocin biosynthetic process; IMP:AspGD.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..337
FT /note="2-oxoglutarate-Fe(II) type oxidoreductase"
FT /id="PRO_0000437072"
FT DOMAIN 179..282
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 263
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 273
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 337 AA; 37912 MW; 7C19987C5999D287 CRC64;
MTKPQPPPIL DFSVFYGHDS QAKAQLVQRV RECCLNNGFF QITGHKVSPE LQRRTFDCAK
RFFDLPLIEK KKIERSPDAF NRGYEAFQSH MSQPGSAPDR KEGLFLGPDL AEDHPYCVQK
KLNCGPNRWP QGLDDLEEFK LVSMEYYAAL FQLAKDVVAV LALTMDYEET FFDPLTEGAI
ATLRYLHYPP QPVGDAEAGL GTGAHRDYSC ITLLLQDGTG GLQVLDEPTG QWLDVKPVPG
AYIVNLANVF ARMTNGHYKS ALHRVVNKSG MERYSIPFFF TGNPDYVCEC LSRFRKEGEP
VRHPPATVHE VVAEAVRGTV ERANRYNAER QGIHAAQ
