EASD_EMENI
ID EASD_EMENI Reviewed; 565 AA.
AC Q5BA81; C8VPT3;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Acyl-CoA ligase easD {ECO:0000303|PubMed:18559263};
DE EC=6.2.1.- {ECO:0000305|PubMed:18559263};
DE AltName: Full=Emericellamide biosynthesis protein B {ECO:0000303|PubMed:18559263};
GN Name=easD {ECO:0000303|PubMed:18559263}; ORFNames=AN2549;
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: Acyl-CoA ligase; 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 -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
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 ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; BN001307; CBF87076.1; -; Genomic_DNA.
DR EMBL; AACD01000043; EAA64654.1; -; Genomic_DNA.
DR RefSeq; XP_660153.1; XM_655061.1.
DR AlphaFoldDB; Q5BA81; -.
DR SMR; Q5BA81; -.
DR STRING; 162425.CADANIAP00009279; -.
DR EnsemblFungi; CBF87076; CBF87076; ANIA_02549.
DR EnsemblFungi; EAA64654; EAA64654; AN2549.2.
DR GeneID; 2875598; -.
DR KEGG; ani:AN2549.2; -.
DR VEuPathDB; FungiDB:AN2549; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q5BA81; -.
DR OMA; VTTHAMF; -.
DR OrthoDB; 683933at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:1900617; P:emericellamide A biosynthetic process; IMP:AspGD.
DR GO; GO:1900557; P:emericellamide biosynthetic process; IMP:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..565
FT /note="Acyl-CoA ligase easD"
FT /id="PRO_0000438972"
FT REGION 284..354
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 355..417
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 213..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 354..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 457
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 565 AA; 62707 MW; 0C7A5CE4EEC2A481 CRC64;
MVFSSPSWVP RIPCEIPDSI PVGQFALEGN TSLPPQCGGR PPFVCAITGK SYSTKVLVDR
VEFLSRSLAQ ELGWSPNEGE PEDKVVGIYS WNTLDFFALC WAVHRLNGIC LPLHPFSIVP
EVVAHMKRAK CRVIFTCQSL VANTLEAARE LSIPGDKIYT TALPEAYLQN PEPIDQFKSV
DQLIAEGEKL QRLPPLQWEK GRAKIQVAYY CATSGTSGKQ KLAKITHYNF IANVMQVCMH
ESYAKNGRNE IAFGAIPLTH GYGLNIGHIM VYRGDTYVIC PRFDMQLMLK TIERFRVERL
YVVPPILAAL AANPFLLDLH DLSSVQATVT GAAALDRSIA AKLNKLRPTW KINHAYGLTE
TGVVATLTSP HDVWHGSSGS LLPSFEIRLV KPDGTDAEGL DEPGEVHFNS PSCFLGYVGD
DESNKNTFDE KGWLKSGDIG VFRKSPNGHA HLFILERIKD MIKVKGEQVL PRDIESVLLS
HPAVIDAAVI GVPDELSGER AKAYIVRSKT VMEDLDEDDL ADEIDEFVQG KLHESHWLHD
RIVFLEKLPK SESGKVLKKD LKAMN
