APTC_EMENI
ID APTC_EMENI Reviewed; 417 AA.
AC Q5B0C8; C8V344;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=FAD-dependent monooxygenase aptC {ECO:0000303|PubMed:18978088};
DE EC=1.14.14.- {ECO:0000269|PubMed:21866960, ECO:0000303|PubMed:18978088};
DE AltName: Full=Asperthecin synthesis protein C {ECO:0000303|PubMed:18978088};
DE Flags: Precursor;
GN Name=aptC {ECO:0000303|PubMed:18978088}; ORFNames=AN6002;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18978088; DOI=10.1128/aem.01743-08;
RA Szewczyk E., Chiang Y.M., Oakley C.E., Davidson A.D., Wang C.C.,
RA Oakley B.R.;
RT "Identification and characterization of the asperthecin gene cluster of
RT Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 74:7607-7612(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21866960; DOI=10.1021/ja206906d;
RA Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
RT "Comparative characterization of fungal anthracenone and naphthacenedione
RT biosynthetic pathways reveals an alpha-hydroxylation-dependent Claisen-like
RT cyclization catalyzed by a dimanganese thioesterase.";
RL J. Am. Chem. Soc. 133:15773-15785(2011).
RN [5]
RP INDUCTION.
RX PubMed=26773375; DOI=10.1016/j.fgb.2016.01.004;
RA Bayram O., Feussner K., Dumkow M., Herrfurth C., Feussner I., Braus G.H.;
RT "Changes of global gene expression and secondary metabolite accumulation
RT during light-dependent Aspergillus nidulans development.";
RL Fungal Genet. Biol. 87:30-53(2016).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of asperthecin, an anthraquinone pigment
CC (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA
CC catalyzes the formation of the aromatic polyketide from acetyl coenzyme
CC A and seven malonyl coenzyme A molecules (PubMed:18978088). Polyketide
CC is subsequently hydrolyzed by the action of the hydrolase aptB into
CC endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then
CC oxidized into endocrocin by the monooxygenase aptC (PubMed:18978088).
CC Endocrocin is likely to decarboxylate spontaneously to form emodin
CC which explains why there is no decarboxylase in the asperthecin
CC biosynthesis cluster (PubMed:18978088). Finally, aptC or another
CC endogenous oxygenase catalyzes additional oxidation steps to form
CC asperthecin (PubMed:18978088). {ECO:0000269|PubMed:18978088,
CC ECO:0000269|PubMed:21866960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,6,8,9-tetrahydroxy-1-oxo-3-(2-oxopropyl)-1,2,3,4-
CC tetrahydroanthracene-2-carboxyl-[ACP] + H(+) + NADPH + O2 =
CC 2,3,6,8,9-pentahydroxy-1-oxo-3-(2-oxopropyl)-1,2,3,4-
CC tetrahydroanthracene-2-carboxyl-[ACP] + H2O + NADP(+);
CC Xref=Rhea:RHEA:64076, Rhea:RHEA-COMP:16516, Rhea:RHEA-COMP:16517,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:149685,
CC ChEBI:CHEBI:149686; Evidence={ECO:0000269|PubMed:21866960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64077;
CC Evidence={ECO:0000269|PubMed:21866960};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:18978088}.
CC -!- INDUCTION: Expression is induced during late sexual development in the
CC dark (PubMed:26773375). {ECO:0000269|PubMed:26773375}.
CC -!- DISRUPTION PHENOTYPE: Fails to produce asperthecin (PubMed:18978088).
CC {ECO:0000269|PubMed:18978088}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BN001301; CBF70383.1; -; Genomic_DNA.
DR EMBL; AACD01000102; EAA57751.1; -; Genomic_DNA.
DR RefSeq; XP_663606.1; XM_658514.1.
DR AlphaFoldDB; Q5B0C8; -.
DR SMR; Q5B0C8; -.
DR STRING; 162425.CADANIAP00007016; -.
DR PRIDE; Q5B0C8; -.
DR EnsemblFungi; CBF70383; CBF70383; ANIA_06002.
DR EnsemblFungi; EAA57751; EAA57751; AN6002.2.
DR GeneID; 2871107; -.
DR KEGG; ani:AN6002.2; -.
DR VEuPathDB; FungiDB:AN6002; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_040697_0_0_1; -.
DR InParanoid; Q5B0C8; -.
DR OMA; WIADCGE; -.
DR OrthoDB; 1519546at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0036184; P:asperthecin biosynthetic process; IMP:AspGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..417
FT /note="FAD-dependent monooxygenase aptC"
FT /id="PRO_5006744329"
FT BINDING 33..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 342..346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 417 AA; 46258 MW; 41CBF494E2DE9411 CRC64;
MTLPVLIIGA GLSGLTTARL LTNAHIPCIV FEASPPSRTQ GYAISLRDWG FNALLRALGN
LPLSSLTRAV APDRHIGGWG WLDQSWRNNQ TGEIIMMPPK ESKEKPTILR ANRNALRQWI
ADAGVGEDEE IDVRYGHRLV GVQLLREGGD GNVVTAEFAN GATYTGSLLI AADGVHSTVR
TLILPAVKPE ILPVLVYHGD FKLSREEYEC VIRPHAGEST IVAGVGDGFN TPLTVCDVTS
TTVHMDWTYS RPSIGDNDPL YNPNITSEEA KVIPEALIEE INAKKLGEPW SLFLNGEAMR
RHRVFNWLTR CVSMERSDVN SCTGKGVVFV GDSWHAMPIF GGEGGNHAIF DGIELAKMLE
VAWGRSKEDV QAAIGKYYDK SWRRCNDAVR RSKQRFYQLH RPISEWIEIA EKQKMRA
