EASC_EMENI
ID EASC_EMENI Reviewed; 479 AA.
AC C8VPT2; Q5BA82;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Acyltransferase easC {ECO:0000303|PubMed:18559263};
DE EC=2.3.1.- {ECO:0000305|PubMed:18559263};
DE AltName: Full=Emericellamide biosynthesis protein B {ECO:0000303|PubMed:18559263};
GN Name=easC {ECO:0000303|PubMed:18559263}; ORFNames=AN2548;
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=18559263; DOI=10.1016/j.chembiol.2008.05.010;
RA Chiang Y.M., Szewczyk E., Nayak T., Davidson A.D., Sanchez J.F., Lo H.C.,
RA Ho W.Y., Simityan H., Kuo E., Praseuth A., Watanabe K., Oakley B.R.,
RA Wang C.C.;
RT "Molecular genetic mining of the Aspergillus secondary metabolome:
RT discovery of the emericellamide biosynthetic pathway.";
RL Chem. Biol. 15:527-532(2008).
CC -!- FUNCTION: Acyltransferase; part of the gene cluster that mediates the
CC biosynthesis of emericellamides, secondary metabolites acting as
CC antibiotics (PubMed:18559263). The biosynthesis of emericellamides
CC initiates from the highly reducing polyketide synthase easB which
CC catalyzes the formation of the linear polyketide chain
CC (PubMed:18559263). EasB produces several polyketides that can be
CC further processed by the downstream enzymes (PubMed:18559263). The
CC polyketides are released from easB as linear polyketide carboxylic
CC acids, which are converted to CoA thioesters by the acyl-CoA ligase
CC easD (PubMed:18559263). The substrates are then loaded onto the
CC acyltransferase easC, which shuttles them to the first thiolation (T)
CC domain of the nonribosomal peptide synthetase easA (PubMed:18559263).
CC EasA then performs condensation of the polyketides with one glycine,
CC two alanine, one valine and one leucine residues (PubMed:18559263). A
CC last step of cyclization leads to the production of emericellamides
CC (PubMed:18559263). {ECO:0000269|PubMed:18559263}.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:18559263}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q70PR7}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of emerecellamide A, C, D,
CC E and F (PubMed:18559263). {ECO:0000269|PubMed:18559263}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA64653.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000043; EAA64653.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001307; CBF87074.1; -; Genomic_DNA.
DR RefSeq; XP_660152.1; XM_655060.1.
DR AlphaFoldDB; C8VPT2; -.
DR SMR; C8VPT2; -.
DR STRING; 162425.CADANIAP00009278; -.
DR EnsemblFungi; CBF87074; CBF87074; ANIA_02548.
DR EnsemblFungi; EAA64653; EAA64653; AN2548.2.
DR GeneID; 2875578; -.
DR KEGG; ani:AN2548.2; -.
DR VEuPathDB; FungiDB:AN2548; -.
DR eggNOG; ENOG502SIRH; Eukaryota.
DR HOGENOM; CLU_026450_1_0_1; -.
DR InParanoid; C8VPT2; -.
DR OMA; WGKPESV; -.
DR OrthoDB; 1130893at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; TAS:AspGD.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:1900566; P:chanoclavine-I biosynthetic process; IMP:AspGD.
DR GO; GO:1900617; P:emericellamide A biosynthetic process; IMP:AspGD.
DR GO; GO:1900557; P:emericellamide biosynthetic process; IMP:AspGD.
DR GO; GO:0035837; P:ergot alkaloid biosynthetic process; IMP:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 3: Inferred from homology;
KW Acyltransferase; Alkaloid metabolism; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Acyltransferase easC"
FT /id="PRO_0000438971"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 479 AA; 52982 MW; B3C43A3B0EC13351 CRC64;
MEETNVKLSV PLSEDVIKLS ALDQQIMRFY AKAVFIFERD SSKTSIDIVH HLKQGLAVTL
SEIPDLAATI APVPNSHRKD LELRIGPNSG VPFKVVDQTK QESWVYGTYP DLAAKHFPTS
DIPHDILFIP QPQPSADGLP AAFLQVNIID GGVIIAISWH HSVCDARGIS ILIDAWARHT
ATSLANGKPD LPATPAEGSR DRWRLDHGLR EVTIDQLPEY TIDSSAREDP SGSYLLDREN
PVTVPYSVST WYFSASSLKA LRDALAQVEN DESTQFTKVE AVSALVWKHM SIARQLDRSN
PDGSSLFTTR LDFRARTKPP FPDTFIGNIN EPTARVRLPI AEICRASTPE SLTTLAEAVR
AATENTTEQS MRTLIGLVND APAVTDVAWK YNYFPGPDLG VTDISNIDAM KKNWGAGLGT
PTCVRSYSRE TGLLYLFPQD DDGGFEIQVQ CEVEAVERLK ADETFTRYCE FKRASAYNA
