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APDG_EMENI
ID   APDG_EMENI              Reviewed;         438 AA.
AC   Q5ATG5; C8VEB7;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Acyl-CoA dehydrogenase apdG {ECO:0000303|PubMed:17369821};
DE            EC=1.-.-.- {ECO:0000305|PubMed:17369821};
DE   AltName: Full=Aspyridones biosynthesis protein G {ECO:0000303|PubMed:17369821};
GN   Name=apdG {ECO:0000303|PubMed:17369821}; ORFNames=AN8415;
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, INDUCTION, AND PATHWAY.
RX   PubMed=17369821; DOI=10.1038/nchembio869;
RA   Bergmann S., Schuemann J., Scherlach K., Lange C., Brakhage A.A.,
RA   Hertweck C.;
RT   "Genomics-driven discovery of PKS-NRPS hybrid metabolites from Aspergillus
RT   nidulans.";
RL   Nat. Chem. Biol. 3:213-217(2007).
RN   [4]
RP   FUNCTION.
RX   PubMed=20828130; DOI=10.1021/ja107084d;
RA   Xu W., Cai X., Jung M.E., Tang Y.;
RT   "Analysis of intact and dissected fungal polyketide synthase-nonribosomal
RT   peptide synthetase in vitro and in Saccharomyces cerevisiae.";
RL   J. Am. Chem. Soc. 132:13604-13607(2010).
RN   [5]
RP   FUNCTION.
RX   DOI=10.1039/c3sc51785c;
RA   Wasil Z., Pahirulzaman K.A.K., Butts C., Simpson T.J., Lazarus C.M.,
RA   Cox R.J.;
RT   "One pathway, many compounds: Heterologous expression of a fungal
RT   biosynthetic pathway reveals its intrinsic potential for diversity.";
RL   Chem. Sci. 4:3845-3856(2013).
RN   [6]
RP   FUNCTION.
RX   PubMed=25494235; DOI=10.1021/ol503179v;
RA   Zou Y., Xu W., Tsunematsu Y., Tang M., Watanabe K., Tang Y.;
RT   "Methylation-dependent acyl transfer between polyketide synthase and
RT   nonribosomal peptide synthetase modules in fungal natural product
RT   biosynthesis.";
RL   Org. Lett. 16:6390-6393(2014).
CC   -!- FUNCTION: Acyl-CoA dehydrogenase; part of the gene cluster that
CC       mediates the biosynthesis of aspyridones (PubMed:17369821, Ref.5). The
CC       polyketide-amino acid backbone preaspyridone A is first assembled by
CC       the PKS-NRPS hybrid apdA (PubMed:17369821, PubMed:20828130). The
CC       assembly of preaspyridone A is initiated by loading of malonyl-CoA onto
CC       apdA, followed by decarboxylation to yield the acetyl starter unit
CC       (PubMed:20828130). The growing polyketide chain then elongates into a
CC       tetraketide (PubMed:20828130). The adpA PKS module catalyzes three
CC       Claisen condensations, as well as beta-keto processing and methylation
CC       (PubMed:17369821, PubMed:20828130). Alpha-methylation step during
CC       polyketide synthesis is a prerequisite and a key checkpoint for chain
CC       transfer between PKS and NRPS modules (PubMed:25494235). The downstream
CC       NRPS module contains the condensation (C), adenylation (A), and
CC       thiolation (T) domains and catalyzes the incorporation of tyrosine via
CC       the formation of the L-tyrosinyl-thioester and the amide linkage
CC       between L-tyrosinyl-thioester and the tetraketide (PubMed:20828130).
CC       The bimodular assembly line is terminated with a reductase (R) domain
CC       that facilitates formation and release of the tetramic acid product
CC       (PubMed:20828130). Because apdA lacks a designated enoylreductase (ER)
CC       domain, the required activity is provided the enoyl reductase apdC
CC       (PubMed:17369821, PubMed:20828130, Ref.5). ApdC appears to operate with
CC       different stereoselectivity in different PKS cycle (Ref.5). Combined
CC       with apdC, apdA is proposed to synthesize preaspyridone A via about 20
CC       enzymatic steps (PubMed:20828130). A number of oxidative steps
CC       performed successively by the cytochrome P450 monooxygenases apdE and
CC       apdB are required for the conversion of preaspyridone A to aspyridone A
CC       (PubMed:17369821). The cytochrome P450 monooxygenase apdE is
CC       responsible for the oxidative dephenylation of preaspyridone A (Ref.5).
CC       Finally, the predicted FAD-dependent monooxygenase apdD and the acyl-
CC       CoA dehydrogenase apdG may be involved in the transformation of
CC       aspyridone A into aspyridone B (PubMed:17369821) (Probable).
CC       {ECO:0000269|PubMed:17369821, ECO:0000269|PubMed:20828130,
CC       ECO:0000269|PubMed:25494235, ECO:0000269|Ref.5, ECO:0000305|Ref.5}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:17369821}.
CC   -!- INDUCTION: Expression is positively regulated by the aspyridones
CC       cluster specific transcription regulator apdR (PubMed:17369821).
CC       {ECO:0000269|PubMed:17369821}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BN001305; CBF80495.1; -; Genomic_DNA.
DR   EMBL; AACD01000153; EAA67037.1; -; Genomic_DNA.
DR   RefSeq; XP_681684.1; XM_676592.1.
DR   AlphaFoldDB; Q5ATG5; -.
DR   SMR; Q5ATG5; -.
DR   STRING; 162425.CADANIAP00002890; -.
DR   EnsemblFungi; CBF80495; CBF80495; ANIA_08415.
DR   EnsemblFungi; EAA67037; EAA67037; AN8415.2.
DR   GeneID; 2868777; -.
DR   KEGG; ani:AN8415.2; -.
DR   VEuPathDB; FungiDB:AN8415; -.
DR   eggNOG; KOG0141; Eukaryota.
DR   HOGENOM; CLU_018204_4_1_1; -.
DR   InParanoid; Q5ATG5; -.
DR   OMA; NECAQCA; -.
DR   OrthoDB; 589058at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..438
FT                   /note="Acyl-CoA dehydrogenase apdG"
FT                   /id="PRO_0000438456"
SQ   SEQUENCE   438 AA;  47824 MW;  13AC0457AD908F2F CRC64;
     MAEISSVPFA EPPYLRGLPS PYYNESHRRF QKACRAFLYE NLLKHAMEWE KAGTVPEHVF
     SDFCKANMLL PNLPAPLPVA WLKRLGIHDI LGVKVEEWDY LHTGIYSDEM ARSGLSGPSG
     SLTAGFAFGT PPIIKYGSKE LQEKFLPDLL TGKKRNCIAI TEPDAGSDVA GITTTATKSA
     DGKYYIVNGN KKWITNGIWS DYSTMAVRTG GPGAGGLSLL VVPLKNYPGV TMQRLKVSGQ
     ITGGTTYIEL DEVKVPVENL IGLEGDGMKM IMNNFNHERL TIAVGVTRQA RVALSTAFSY
     CLKREAFGKT LMDQPVVRHR LAKAGAELET MWAFVEQLLY QLTNLPKEEA DRQLGGITAM
     AKAKGAMVLN ECAQTAVLLF GGAGFTKQGQ GELAEAILRD VPGARIPGGS EDVLLDLSIR
     QLVKLFKAEE KKLGKARI
 
 
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