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Database: UniProt
Entry: A0A0A2IUY4_PENEN
LinkDB: A0A0A2IUY4_PENEN
Original site: A0A0A2IUY4_PENEN 
ID   A0A0A2IUY4_PENEN        Unreviewed;      2464 AA.
AC   A0A0A2IUY4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Acyl transferase/acyl hydrolase/lysophospholipase {ECO:0000313|EMBL:KGO58154.1};
GN   ORFNames=PEX2_066640 {ECO:0000313|EMBL:KGO58154.1};
OS   Penicillium expansum (Blue mold rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO58154.1, ECO:0000313|Proteomes:UP000030143};
RN   [1] {ECO:0000313|EMBL:KGO58154.1, ECO:0000313|Proteomes:UP000030143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-8 {ECO:0000313|EMBL:KGO58154.1,
RC   ECO:0000313|Proteomes:UP000030143};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO58154.1}.
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DR   EMBL; JQFZ01000121; KGO58154.1; -; Genomic_DNA.
DR   RefSeq; XP_016599648.1; XM_016743935.1.
DR   STRING; 27334.A0A0A2IUY4; -.
DR   GeneID; 27679355; -.
DR   HOGENOM; CLU_000022_31_1_1; -.
DR   OrthoDB; 5396558at2759; -.
DR   PhylomeDB; A0A0A2IUY4; -.
DR   Proteomes; UP000030143; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
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; 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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Hydrolase {ECO:0000313|EMBL:KGO58154.1};
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:UP000030143};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO58154.1}.
FT   DOMAIN          20..437
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2377..2455
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2464 AA;  269297 MW;  689C871A4EE21978 CRC64;
     MNSTTGQGQS SCRNHEDDFG EPIAIIGMAM RLPGGVRCGD EFWDMLVNKR DGFCEAPPSR
     CSREASSSPD CGDLREMKKG FFLQEDPACF DASFFSVPPH EAARLDPQQR LLLEVVWECL
     ENSGETKWRG EKIGCFVGVF GEDWLEISHK DPQHLNQIYP IATGSFALAN QVSYRFDLLG
     PSMTIQTACS SSLVCLNEAS QALRSGECST ALVGGTSLIW GPTMTDAMTK NMVLSPSGIS
     HTFDADADGY GRGEGINCIY LKPLRDALRD NDAIRAVIRS TVTNHDGKTP NFSQPCPISQ
     ERLIRHAYQI AGIDAIHETP VFECHGTGTA VGDVIEASVV AKMTQGEVTY ITAVKPNVGH
     SEGASGITSI IKSILSLENK TIAPNIHFKT PNPQIPFQDA NLHVPLEPTL WPAGRPQRIS
     VNSFGIGGSN AHAILESAST ISPKSQNASL GISDPQLLVI SAHTVETLRK RIAQIVDYVK
     NHPSRIHDLS YTLAARRSHL PHRAFAVVHP TKATIDDTAF TIFNTSSPSV TFVFTGQGAQ
     WPGMGLRLLS SFPIFKEDIK IMDEALQQLP DGPNWLLYDE LRQESSISRI HEAEFSQPLC
     IALQIGLVNI LRGWGIEPST VVGHSSGEIV AAYAARAISM RTAIIIAYYR GKVAKPLEGS
     GAMVAVGLTP DEVVPYLTPG VVVACHNSPH SVTLSGDKDS IDRAIKNIKA ANSDTLCRRL
     TVKIAYHSDH MKQIGSEYEH CISHHIEYEE AMLPFCSSVT GDTITDPRKL DASYWRQNLE
     SPVLFTEAIQ SLPTSGTPVF LEVGPHSALA APLRQIFRIL SARSPVYIPT LFRYEEDVQT
     QLLCTAGQAH ATGLGVNLSS ITELGNTLTD LPPYPWQHDR PYWSESRLSR EWRQRAFPHH
     EVLGSRVVDT TDHEPSWRNL VTLDNVSWLL DHLIQGAVTF PGAGFVAMVG EAVQQLHPDN
     DSYSVRNMTF ITPLLFHEGD QIEMVTSLSP VEVADRVPSG WYGFKIMAHD GERWTMHCQG
     QVRAGSDHPP ESFPISSYKR SVPSEGVYRV LQRSGIDYGS QFQGLEKITA DPTGPRATAT
     VLGNRGLPGS RYSLHPTAID QCLQLMGVAC SQGLLRHLTT IYVPAMIDSL FVGSGGPPMS
     ASARTKRGTR DGQLGDAIAM LGDKVVLSIQ GAYLFALEND NIDSGTGVAG SLAHLEWKSG
     IDFLPLSALL STPLDYTAQA MNIKALGQIS VLFVLETADK IEDVEPASPH SAKWKKFIID
     AAFNIKTSGR QSIYPESPQW ALLSSSDRQE MIRKVLAETK FTFDAPLVDC TQVVFDNCIA
     FTSGESNPLE VLVKDNLLHK FHGAHTQYAD WKPFLPLLCH SNPGLRILEI GAGTGSATAM
     ALELLKSPSG ERMYSQYVFT DISSGFMAAA TERFGHEQGM EYKVLDITLD PLEQGFDAHS
     FDLIIASNVL HATPSLHPAL CYVHLLLKPT GRFLLHEICP EILTANFTMG VFPGWWLGED
     DGRSDQPYIS PERWDRELRA AGFTGADVIA YDHKPPYHVS ASMLSRPVDE ITIPNDIWLL
     KSNSTPCEWA SDVELQVRDK GYITNWTTLH ETPPQGKFVV SLLDLQGAPI GSLPKDDYEV
     FQRYIEQAQE CQILWVTQST SHTCSDPIFG FIHGLARTLR AELLLDISIL EVPAWDTASA
     KAVVQVCEKI QRSRAQSLPD PEYEFALHEG EIKVGRYHWT PLVEQLASPP RSDSSRKLAL
     TTYGLLDTLH WAEKEASYEL NEEHVEVEMD YVGLNFKDMM VAMGFFGNKE DLGLEGSGIV
     LRVGADVTDI TVGDRVVLMH SGVLASNVVV PHEACIKLPQ GLSMADAATM LTAYVTVLYS
     LLEIGALKKG QSVLIHSACG GVGLAALQVC QAVGTEIYAT VGNEKKVAHL MEHFGLPRER
     IFNSRNTSFQ PDLMRATAGR GVDVVLNSLS GNLLHASWEC VAKFGRMVEL GKRDFISHGM
     LNMSLFEANR AFFGVDLAQV CKETPKILKS TLATFSDWYR QGKIGPIKPV KVFDAIDIVS
     AFRYMQAGTH LGKILVRMPT SVESLPPPVV KTFPTFRSDA AYLLIGGLGG IGRSVSTWMV
     EQNARELIFL SRSAGKSEED QAFIQELETQ GCQVICVPGN VTNLNNVKEA VATCTRPLAG
     ILQMAVDLND RLFLQMSHEE WEAALAPKVA GTWNLHHATL KHSLDFFVVF GSIAGVCGNT
     GQANYAAATT FLEAFTRYRR QQGLPSSILH LGVVGDVGAA SRNSRFLQRI QSIGLHVLHE
     GEVIDALAAA INISPVSGSN ATGAMAMGLA HTRRRADLPK EIFLGGRDAR FSIYPNLEST
     SDGIGGDSSS HANALKALLA QIQADPSLTG KKETEVALMK ELGKFISHNL TGQTQEEGPD
     SADDTEALAG MPVDSLMAIE VRNWLRRSLG LEIPTVEINR AGTLGGLVKV VLKGLGEKYD
     QRAT
//
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