EASB_EMENI
ID EASB_EMENI Reviewed; 2534 AA.
AC Q5BA83; C8VPT1;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Highly reducing polyketide synthase easB {ECO:0000303|PubMed:18559263};
DE Short=HR-PKS easB {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:18559263};
DE AltName: Full=Emericellamide biosynthesis protein B {ECO:0000303|PubMed:18559263};
GN Name=easB {ECO:0000303|PubMed:18559263}; ORFNames=AN2547;
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, DOMAIN, 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: Polyketide synthase; part of the gene cluster that mediates
CC the 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 -!- DISRUPTION PHENOTYPE: Impairs the production of emerecellamide A, C, D,
CC E and F (PubMed:18559263). {ECO:0000269|PubMed:18559263}.
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DR EMBL; BN001307; CBF87072.1; -; Genomic_DNA.
DR EMBL; AACD01000043; EAA64652.1; -; Genomic_DNA.
DR RefSeq; XP_660151.1; XM_655059.1.
DR AlphaFoldDB; Q5BA83; -.
DR SMR; Q5BA83; -.
DR STRING; 162425.CADANIAP00009277; -.
DR EnsemblFungi; CBF87072; CBF87072; ANIA_02547.
DR EnsemblFungi; EAA64652; EAA64652; AN2547.2.
DR GeneID; 2875599; -.
DR KEGG; ani:AN2547.2; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; Q5BA83; -.
DR OMA; RNWIGAY; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1900617; P:emericellamide A biosynthetic process; IMP:GO_Central.
DR GO; GO:1900557; P:emericellamide biosynthetic process; IMP:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2534
FT /note="Highly reducing polyketide synthase easB"
FT /id="PRO_0000438970"
FT DOMAIN 2452..2529
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:18559263"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..473
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 587..885
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 973..1273
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 1395..1625
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 1834..2146
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT REGION 2453..2526
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18559263"
FT COMPBIAS 18..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2489
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2534 AA; 278404 MW; 0BA63D1B4782F280 CRC64;
MSPASRSRVE IADSESDSER LSSSPWSILS DNDSNTSDER STRAGPGSLE PIAVIGIGCR
LSGSATDVSG LWDMLKSGRS GWTPGPGTRF NMKAFQDPTG TRSGTTNATG GHFIREDISK
FDATFFGINP VEAQAMDPQQ RLMLEVAYEA FENAGITMDA LWGSNTGVYV GQWASDYHEI
ATRDIERPPL YLVTGTGPAI TSNRVSYVFN LRGPSFTVDT GCSSSLVALH QAVLSLRNRE
TTQCFVGGVN LLLDPQRFHY QSRLKMFSKD GRSFPFDARA NGYGRGEGVT GVVLKPLSVA
LRDGDPVRAV IRNSVLNQDG RTPGISVPSA VAQKEAIIRA YRQAKLDLYA DYVEAHGTGT
KVGDPIETSA IAAALTQRRS PSRPLPIGSI KGNIGHTESA AGLAGLIKSV LMLENGMIPP
QVNYETTNPD IHLEEWNLRI PTKLERQTLR RISLNSFGYG GTNAHVIIDA AHEAISAFGR
LSLSRHLQLS YHSEKPRVFM VSGASEKACQ RVCARLARYL VVNHRNSINP DALLARLAHT
LAKQSIHAYR VIFVASELDE LIKQLITASH STITRREKFG QHRIALIFSG QGAQYAEMGR
DLLKSYPSFV RSLERARQQL SRLGCTWDLL SELCRPKADS RVNEPAFSQP MCTAIQLALV
DLLNEFGVSP SAVLGHSSGE IGAAYAAGAL SFRDAISVSY YRGKLASELL AENQSPGAMI
AVGAPPDIAE QHINKLGTDV GRMRIACFNS PSSVTVSGDV AAIDRIKEVL DTEGLFNRKL
ITHGAAYHSH QMKLIEDKYI AALKGLKAKP VSSSIRMFSS VTSKELDEST VLDGGYWAQN
LVSPVLFSQA LRTMCEQDYN GLPIDTLIEV GPHSQLSGPV NQILKTIPGP HGQASYTNTL
KRGDDAETAL LRCLGFLAIK NGSVRLCDLN KDSKDSDIQP LADLPPYSFD HDRSFWHETR
LSRDYRHREH LPHELLGTLS ADVNKLEPRW RRFVSLKETP WLRNHIIQGL ITFPAAGYIT
MAIQAIRQHM HTANPASTIQ FIRLRDVSFG KGLVLPDENA EVEISLSLRP QARTARESSG
IWNEFRIFTV TPDQKWTEHC RGLVQAEVDS VEGFRSIFTP ADISRIDSEC THGTIPQKFY
AVGKRNGLDW QHPFNNLHQI RSSKHSCVAT ARVPEYEMPS GGMEDLLHPA VLDSALFHGL
STVIYLEDGR SSAYVPTFIK QLWVANRHVA PGSYLTCSTI RRNEPLVFDL HTKDEINQMA
VVAQGIRVTS LGGDVAAGVS KREACHTQTL VPYVDAWTTE HRDQVCRATI ELGSLMETNR
ALDAITIHFA QNAIREISLN DIQETHLQRY FQWMGTLADE TYDNILLENK PEDLGVIGEA
IAILGPHLVD ILKGKTSALS LLTKNNLLSR VYTEWCSSRL YPQMSAYCHE LGRFNPQLKV
LEIGAGTGSA TLPILKALND CSGRFIQRYD FTDISPGFFE PAKERLGDLA NVVEFRVLDA
GRNAQEQGFE EGAYDLIVAC NVIHATPRID ETLRNIRPLL KPGGKFMLME ISRYTLYFNI
VFGLFEGWWL GYDEGRTRSP LLTDSEWCQR LEKAGFAHIE KAFVDYPHEN GGSLSVFIST
APFPRRNESL PIHLLTDSNA SNATEEQAQE IQQACQTSVA LLPITHPCQH GGVAILLPEI
AKLLCAEPDV NVWNSFKNWI LKSRAVLLVS NCTMADSSHA ETGLWAGFAR TMRLEYPNLR
QVVLDIQTPN VPVMSKLKEV LPIILNSSSF DLDCLSSEVE NEFTEKDGQL FVSRYAYRPD
ISRDVDLTSR QAASEPVPFV STGRILTAEL GVPGLLETIR WKDDIECPPL GPDDVRFELR
GASINFKDVL IAAGQLEGIT EMRNDCSGVV VEVGENMKHR FKPGDRVCAL YSRSYTNYPL
VHGDCCQVIP DSLSFAEGAS LPIVWATVYY GLVDKGSLSK GEKILIHSAA GAVGQAAIML
AQHLGAEVFA TVGSEAKRDL LHAKYGVPYD HIFSSRTTAF YGEIMKSTGG YGVDVVLNSL
SGEMFRESCN LMASFGRFVE IGRKDLMDDA LMPMEFLLRN ITFSYVDLTA IIEQRKPLAR
RLLHDIADLA ASGSIRPVTL TTMPISDIEI AFRQIQAGKH TGKIVLTVEE NQEVPAVPSM
PKQARLHEDA SYIVVGGLGG LGRWLTTWLA DHGAKHIVAL SRSGAKDADS RTFISNIRGR
GVNLIAPPCD VVCADAVVAL AQELKRSELP PVRGVINSAM VLRDTLFDNM TEDDWRTALA
SKVRGSQNLH TTFKSLDFFV MMSSIVAVRG NYGQSNYSAA CSFQDTFVRH MVQQGEPAFS
INIGPIRDVG YVSENPEVAE ALRRNGLGSI GVSDVLIVLN HAILNARGAN PSTCVASIGL
IASDDESENG RDFLMTDRRF SQLVKHNGSK QKSAGEALDA ITLLSAATQL DEAVHIVTNA
ILNQLSKLIV TPVEMLSPAQ SLDSYGVDSL VAVELRNWIG AYLHANVQLM VIRGTGSISQ
LAAIVAKESR VVKL
