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Database: UniProt
Entry: Q5AS20_EMENI
LinkDB: Q5AS20_EMENI
Original site: Q5AS20_EMENI 
ID   Q5AS20_EMENI            Unreviewed;      2449 AA.
AC   Q5AS20; C8VLK6;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   SubName: Full=Polyketide synthase, putative (JCVI) {ECO:0000313|EMBL:CBF84683.1};
GN   ORFNames=ANIA_08910 {ECO:0000313|EMBL:CBF84683.1};
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 {ECO:0000313|EMBL:CBF84683.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
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., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M., 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., Hynes M., Paoletti M., Fischer R., Miller B.,
RA   Dyer P., 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] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
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).
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DR   EMBL; BN001307; CBF84683.1; -; Genomic_DNA.
DR   RefSeq; XP_682179.1; XM_677087.1.
DR   STRING; 227321.Q5AS20; -.
DR   EnsemblFungi; CBF84683; CBF84683; ANIA_08910.
DR   GeneID; 2868230; -.
DR   KEGG; ani:AN8910.2; -.
DR   VEuPathDB; FungiDB:AN8910; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_1_1; -.
DR   InParanoid; Q5AS20; -.
DR   OMA; CFRYMQK; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
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   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 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; PF21089; PKS_DH_N; 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; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          18..437
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2353..2430
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2449 AA;  269315 MW;  0B8C5F397020BC2F CRC64;
     MSETTPQTGR TTSASWADDP IAIVGVGLRL PGSIRTPQQF WQFLVNKRSG RCRVPADRYN
     VDAFHGPKGK LGHVCTEYGH FLDVDLAAVD SSFWSIPPKE LLLLDPQQRL LMEVVYECLE
     SSGTAAYRGR DIGLYIGALG EDWMDIQTRD PQGLGMHCVA GYSDFALSNR LSKELGLTGP
     SMTIRTACSS SMMALHAACQ ALYTGECSSA VVGGCNLILS PRMTTTMSEL GVMSPTGDCR
     SFDARADGYA RGEAVNAIHI KRLSHALRDG DPIRSVIRSV CINSDGPRSP VFIPSPESHE
     LLIRRCHQLA GISDLSQTAM IECHGTGTKV GDVQEGRAVA NVFGDIGGVL IGSVKPNLGH
     SEGASALTSI IKMTLALENQ TIPPNINFST PNPKIPFGPA CLRVPVECEP WPKDKAERVG
     LNGFGIGGAN GHVLLESARS FLGTFVNEAP SGCTPQLLVF SGTHPETVKR NISLSLDFLA
     KNPAKVADAS YTLACRRRIL PNRAFAVGCL DSWDVSPVRK AGPADLVWVF PGQGAQYPEM
     GLKLVTGNAI ARDTIRSLDE VLDLIDAGRS WTLHDELLRP EPSSRLSQAK FSQPCCTAIQ
     IALINVLKSM NVKPSAVVGH SAGEIAAAYA AGALTAAEAM AIAYQRGNIA ERVEGSGGMI
     AVSLSREQVS PFLTDQVTVA CENSSRNITL SGDSAALDDV VEKLQCTYPE VTTKRLGVNC
     AYHSEHMNIV KDEYLDRLVA LKVKQQPLST TFVSSVTGKS VENAGDLDTE YWCRNLVSPV
     LFYSAVKDTI AALPNPVFLE IGPHSALSGP LRDISPSTPY IPTLVRGISA NTSILRTVGR
     LFQFTEIDLS GLVTGSVLTD LPPYQWQYDR RFWSESRVSR NWRFRQHPHH DILGSQIPDG
     NEMEPLWRSL IHLDSVPWLR DHVIDGKTVF PRSSYISMAG EAIRQLTGSS DVSLRRVSFL
     EDITFDGKHP TEVLTQFRPI QGTEWYDFTL TSQFEGKWTK LCMGQARRGY DLPSDIKQLC
     PGHRKVKPET FNRAMERLRI IYGPRFRALD RIAVNATAPE ATAEITERHE RQESHYIVHP
     CTTSSIFQLL TIAKAKGRNF DHSFVPTYIE EVYVTASTGS ISAQSIITAT QNRTFSGDAA
     GFCGGSLVFF MRNIRLMPTE NRYDRGLDPH AGARLVWQPD IDKAHLARLI RPHCDKSILE
     NLFLVEELAL ACIIESEQQT RSSKALAHFA RYSEWLSLQR QRAEQGNYDH VKSCQAIASM
     PSKDRGNHIK ELYQKALMTP VQHVATAVMR IYHETTTLFA GQVDPLSILM KDDLLSAIYG
     FNLCDFADFF RVIAHNRPCM RVLEIGAGTG GITATILPAM HTPHGERLYH SYTYTDISSG
     FFERAQERFR AYKGVDYRVL DISVDIAAQG FDAPYDLIIA SNVLHATPNL QQTLANVKAL
     LKPGGKLFLQ ELAPTTKWVN YIMGTLPGWW LSNDDRPWEP YVSPKRWDAE LRAAGLSGAD
     TVVHDGHMNA HIVSSLPELR SERNRQVTVL CKPGSEHLNS VIAYLHTRDF VTDTRHLGEE
     LPNNQMVISL LELDGPQLHA MNETEYLNLR DLITSLDQKT MLWVTRTSQV ACSDPRYAAT
     LGLLRTARRE LGLTVATLEV DTLDVKAIDA IAEVTERVLR LETTSSLDPV LEYTHAYGTL
     MVGKYYPAIV SEELLDRAAS DQTAAVLRTS PRNIETLTWE RMSLEISAPV EDWVLVETRA
     VGMNLKDLLV VNGTLDAALG SECAGTVQRV GPGVKNLRAG DRVMVLSPNS GVMATKFVTS
     ERLCARMARN LSWTEAATIP FAFATAFYAL IDVARLKYGD SVLIHHACSE IGTAAIQICR
     MIGAKFYCTV AKRADEDYLL QLGIPKERIF SSRNSTFVRD LMVPTAGLGV DVVLNTLSDN
     LFHASWQCVA EFGVLVDLPQ GEFNKQLPME AFEGNRSFCA VNLSQVAAKR PETIQGLLRR
     CMHHYALGEL TPLQLQEFPA EKAQDAFKSM KEGKTGKAAI IMPEESSSLP ACFSRREPSF
     RNDAIHLIVG GLGGLGRSVS SWMASHGARH FVFFSPSAAS KENDDFVLEL RAQGCRLDLV
     SGDISNPEDV DMLIKGLDEN IPIAGVMQAS MALEVTSFAT MSFAQWQAAF APKCQGTWNL
     HNTLLKYSRK TDYFLLFSSL SGLIGQTGYA NYAAGNAFLD AFVQYRHSLG LPCSAINIGV
     MEDVGYVSEQ THAIDHFVAT STYTLQERDL HDAVQLAIDK SSPVGTTTRN GPAQPTYVNE
     SQLLIGLRST APLDSPNNRT SWRRDPRMAL YHNLNQSAAK SASEKTTDTA DDQILVCFLE
     QLKGEPDILD KPESIDLLST EIGKTLFSYM QRDRSNLDLD VPLPSLGVDS LLAIKMRNWF
     QRKIGVDIGV VQILNSGSLR DLGRITAKAI AGLRIAESTV SVADLTPMS
//
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