ID A0A0A2JBQ0_PENEN Unreviewed; 2645 AA.
AC A0A0A2JBQ0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Acyl transferase/acyl hydrolase/lysophospholipase {ECO:0000313|EMBL:KGO52789.1};
GN ORFNames=PEX2_083230 {ECO:0000313|EMBL:KGO52789.1};
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:KGO52789.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO52789.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO52789.1,
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:KGO52789.1}.
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DR EMBL; JQFZ01000259; KGO52789.1; -; Genomic_DNA.
DR RefSeq; XP_016595492.1; XM_016745593.1.
DR STRING; 27334.A0A0A2JBQ0; -.
DR GeneID; 27681013; -.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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: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; 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; 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:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 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; 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 Hydrolase {ECO:0000313|EMBL:KGO52789.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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:KGO52789.1}.
FT DOMAIN 10..441
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2562..2639
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 460..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2525..2555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2645 AA; 286842 MW; D495C7C398DB0C03 CRC64;
MDTENSEWAS EPIAIIGMSC KFSGGASNPD KLWDLMASGK TGWSEIPEDR YNIKGVYHSN
HERTSTTHVK GGHFLEDDVA AFDAAFFNYS AEMAQVVDPQ FRLQLESTYE ALENAGLPLS
QVMGSQTSVF AGVFTHDYQE GIIRDEDRLP RFNVVGTWSP MSSNRISHFF DFRGASMTLE
TGCSTTLVAL HQAVHTLRNR EADMSVVTGA NVMLNPDTFK AIGSLGMLSP DGRSYAFDSR
ANGYGRGEGV ATIIIKRLSD ALAANDPIRA VIRETALNQD GKTDTITTPS GAAQIELMQE
CYRRAGLDPR GTQYFEAHGT GTPAGDPIEA GAMAAIFGGG EGRDNEENYL RIGSVKTNVG
HTEAASGLAA MVKGVLCLEK GLIPPTVNYE TPNPKLKLDE WRLKVVRTIE QWPDSLVDGP
HRMSVNNFGY GGANAHVILE SADPWTLTPG LDLSPVNGNG SHSVNGNGHS NGNGYTNGSY
HTNDTTDDTK VLILSARDER GCQQMASDLK AYLKKHKSLG HEASEQLLRN LSYTLGERRT
LFQWVAAYQV RLEKDDTLDA AIQALDSPRF KPGRRASDSP RIGMIFTGQG AQWYAMGREL
LSSYPVFRQS IEEAEAYLHA LGADWSLLEE LQRDRKTTRV HDTKISIPVC VALQIALVRL
LEAWGITPSA VASHSSGEIS AAFAVGALTH RQAIATAYYR AVLVADETKR APGAAEGAMA
AVGLGVEAVQ SYLDRVTTAN GKAVVACVNS PQSVTISGDA DAVQEIEDLC KEDGVFARRL
KVQQAYHSHH MDPFADAYRE CLRVEMARGV AQSSKQHPQA AKQQLKAVFS SAVTGGRITD
IKDLANPDHW VGSLVQAVEF VDAVTEMVLG DPDDPTGRSV DVLLEVGPHT ALGGPIREIL
SLPEFEGLEL PYWGCLVRDE HAGDSMRSAA INLFREGQSL EMNQINFPVP AYDDESPQVL
TDLPSYPWNH AMRHWQESRV NRAIRERSQP PHELLGMPVA GNDPSSAVWR RMLRVTETPW
VRDHMVQGSI VYPGSGYICL AIEAARQLEK AGTTNEGISG FRLRDVNFLF ALVIPDSAEG
VEIRTTLQSV PEREIGARGW RRFEVSSVTL DNRWTLHAKG MIMVEREATA IETAEHRPLS
TYTRQPDPYD LFANLRARSV YHGPLFQNTT KIIQDGLEPR SVCDITIRHE VSSDTDPVVA
AQNTLLHPIT LDAVVVAFYS VLPSVGALQE DPKLPRSIAS MWVSSNISHE IGRTLHCDTS
LLHDDAQSGL ADITVFDGQT DATVLKIQGV ELASLGRGSG ATARQDAANK GGAAITSKWE
QEVCSKLVWG PDLSIRNPLA LAQIKKQLVP TDSDADAEIA RNLQRLCIYF AHDALQALTS
EEVAKLQEQP HLANYYAWLH DLTAKATKEL ALEGPQERQQ CIAATTSQSV DGKLVGRLGP
LLPSILRGEL KLEEVSGLLN EYNANAMRRS SALRQLSALL RKVAHKNPGA RVLQIGTGTG
AHATRRILEA LGTPKTPLVA SWHITEPSSE SLEDARAQLA DWADLLEFDQ LDIEQSPAKQ
KFTPGSYDIV VAFQALRATK NATSAVANVR SLLKPSGTLL FAETTNDQVD VDFIFGLLPS
WWQGEESDRP TPTASSWDNV LRDAGLSGVD LEIPDSESDI IHTNSIIMST VPLVEDQKSN
LGKANNGESF VVVTSSKTPP PPGFVDLLSR RIQALIGADT VTPEHLVLEQ SSFDTYKTKI
CVFVGEIDKP IMADLDAARM EGLRAMVTQC SGLLWVTTGG TVESEAPERA VHQGFLRVLR
NEYISRRILS LDLDPAHAAE RWSSGGDAVV SAIVQVLEEG FGRADTEAGP TEFEYAERDG
VLQVPRYYKD EQYNDMVTGP LVPSWSEVLP VAKDEKGSID AISSIPLEPL FQEDRPLRLE
VGIPGHLDTL AFTHDKEEHE ELTPELVEIT PRAYGVCSRD IVAAMGQIKD RSMGLECAGI
ITRVGTEAQA KGYNVGDRVM ALLTGASFAS RAYVPWHGVI QIPSDMDFVN AASLPLAFTV
AYAGLVDTAR LAAGQSVLIH AAAGAIGQAA IMLAKHIGVT EIYATAGSQE KRDLLQREYG
IPAERIFTSR DASFAPAVLA ATKGRGVDIV LNSLPGLLLQ ASLSAIAPLG YLIEIGKKDI
EGNSLVALES FSRGISFTSL DVPTFLRRRG PDVHRALGEI ARLIEQQVVK PVHPVVIYPM
QDAQAAFRFV QTGAQMGKVV LLTGTEEQVH MVPQPKGITS QTQLRPDASY LIVGGVGGIG
RSVAHWLVAH GAKNLILVSR SAGDLDLVKN KNTDGALFIR ELREMGCRVK PISCDISLAS
SLTVALRVCE NDGFPPVRGI IQGAMLLRDA IFEQMTLEDW SSGLRPKLYG TWNLHTEFSQ
PGSLDFFVML SSVSGVVGIA SQTNYAAGGS YEDAMARWRQ SRGLPGVAID LGPISDIGYV
STSSKVAERL RKDGDFAMLD EDIVLRALNA AVLHPLGARS QIIVGLNSAP GPQWDVNGRS
QLGRDARFAP LRPRSKASAR PDGESNGASL SAQLAEASDP QEGAELIGAA IAVKLADIFM
TPVEEIDLAK PPAHFGVDSL IAVELRNMLV LQAAADISIF NILQTASLAA LAGLVAEKSR
HLQDA
//
