ID K9FPB6_PEND2 Unreviewed; 2542 AA.
AC K9FPB6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EKV11465.1};
GN ORFNames=PDIG_49980 {ECO:0000313|EMBL:EKV11465.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV11465.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV11465.1}.
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DR EMBL; AKCT01000204; EKV11465.1; -; Genomic_DNA.
DR STRING; 1170229.K9FPB6; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; K9FPB6; -.
DR OMA; EYGIDSH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 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; 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; 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; 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; 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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..454
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2542 AA; 279319 MW; 6F6F2BDE0A1F42B2 CRC64;
MSQRVSVKHP KATISEHDPA NTAIGFCTPI AIVGIGFRGP GNAKNVEELW EMILNRREAW
SPIPPKRWNS AAFYHPDNAR HGTINVEGGH FLEEDVSVFD APFFNMTSDE AAAMDPQQRL
LLEVTYEGLE NAGIPLTKIM GTKTSCFVGS FSADYTDLLL RDPECVPMYQ CTNSGQSRAM
TANRLSYFFD LKGPSVTVDT ACSGSLVALH LACQSLQTGE SSTAIAAGVN LILSHEFMST
MSMMKFLSPD GRCHAFDEKA NGYARGEAAG CLILKPLAKA LHDHDKIRAV IRATGSNQDG
RTAGITLPNG AAQEKLIRSV YARADLDPSE TDFVEAHGTG TQAGDPVETG AIARVFGAGR
SPDNPVRIGS IKTNVGHLEG ASGVAGVIKA VLMLENRTFL PNRNFEKINP RILLNDWKLK
VQLQPEPWET TGPRRVSVNS FGYGGSNAHV IVEDAQACLS ELGLQGHNGI PSNIAKSHGE
KLPSPPLGTP RVLMLSGFDE RTCIQQMQAL SNHILDRGDE VDHAKFLNDL AYTVNERRSV
FPWKAAVVGD TLAGLAASLS RNFKTKSTVR KPTLGFVFTG QGAQWARMGK ELLQAYPVFK
LSILSIDEFL EGIGASFKVE GEIAKCTQDS NLNHPSLSQT VCTALQIALV DLLASWNIHP
DSVTGHSSGE IAAAYAAGAL SMKDAMSVAY YRGAVASQLL VAQPNRGAMM AVGMSAEEIQ
PYLDRFQSRQ LVVACVNSPS SVTISGDMSA IDALAHTLKE QQVFSRRLDV GVAYHSPHIE
QVAENYRSLI DHIKPHGLDP IVGDKRERPG SFFSSVTGTI IPLRELDAQY WVSNLVGQVN
FAKSLRSLCF DTYGQRAGHI GVSRTRRAGT AQKPSVDCLL EIGPHAALSG PIKQVLQADA
KLNAADIVYI SILTRKVNAV TTALGAVATL VSLNYPIDFS AINRPMGTEF SSAPQLLVNL
PTYAWNHTRS YWAEPRLSKM YRNRRSPRMD LLGAPDKMAC PFEPRWRNYL RTSELPWLLD
HRIQGNIVFP AAGYLVMAIE ASIQLNKDEE RVTKYILRDV VIQSALVLNE TSAVEIMMSF
QKSTQDQEQL YNFHIYSISK ENRWIEHCNG LIGTQKSIGV SGNGVEETDG YATVPLGTEV
HGISVIDMHD FYKKLQVSGL EYGPYFANLT KASVTQDGAC FAELTVPDTL SVMPASFQHE
LLVHPCTLDT IFQTVFAALP LGMGIEEGPA VPVSIEEMIV TSSLSCSAGE LMSICTQVRP
MPNKDVKACI IAVNCNEKQF ETEPAISIRG LRCARLERHE PASQAKDNRI IYQIDWKPDP
SFLSSQNGSF FFNKNDPVQE LAPQTEYEEN AAEFIRAALE DVGSTEAMEL STSHRRFWCY
LQDLLERHDE NPSKSSSHLE DIRSPSMGSL LPIVGKSLVA IIRNQVDISS LFQEDRLLDE
FWDIFSADES YQVAAKYVNL IGYGKPDISI LEFGVGTGQV AEIFLNHLVT KNETPHCGKY
TFAHESDSVI EYTLKRLEKW SEWVECKPLD LGNDFPKQGF EENSFDIIIL PHGLCTASCE
QSALSRIHGL LRQSGYLIAV NPFDPKNNIV KSLLFSALHC LSADKFCLGQ GAWMKSQWNE
ILQDAHFTEV DAYAEQDSEK SHQFIVARKR NIQKSTRMVS IISKEKAEAA RHLVTELEKI
SCEVNVTHID NVECKDQICL VLDTSVSSML AAPNEITFNK IKTIFTKSGG VLWITKGGAI
ESVNPNAALA VGFARTARAE SGVNPIVTLD LDAQNLLSEY QTAKMIAKIL VTRFLRENPD
GDTEYAERNG QILVPRVLEH LEANKTMNSI TDTDVISELN FHQLQQPLRL SRKLDNPPGF
VVDSQMTELP VGCIGIEVHS FGLNKWDFQP DYLDWETDDT LGLECSGIVY KVGAGVHGIT
VGDRVACLGA GTARSFYHDR ASAFQRIDDE MTLQMASALP LAYTIAYYVV NHLSIVESND
AILVHDAGSH FGQALLEVYL LKDARIFATV QNPSEKGLLS SKFGIPEGHV FISGKDDIAK
EILRLTDGKK ANIVVTFETA DDKVLQSCTA KFGRFIQLRT SKLKSRLLSC PPNTSLSTVN
IFELQKERMD LANRIWPKVF RYFVEGRLKG PGFIDAHHVS HIQDAIMAAQ SRQHVVVHVE
ENDLVKATLP KSTPPLFHAN ASYMLVGGLG GIGRVVALWM AENGAKSLIF VNRSGLSKYQ
AQMTVRNLVE KGVQITTRAC DISDETEVQQ MIHDLSYCAP PIRGLIQAAM VLKDVHIENM
RLDEYRDVTG PKYYGTWNLH RHLPTDLDFF LMLSSISGVI GNATQAAYAA GSTFMDAFAA
YRRSLGLSAA SLDLGTITDV GHLAENQDLA VKMERQGFQG TDVITLLSLI QVAISQSTSG
GAQFVTGLGR WKETVSLGNF NAPLFSHFRF KFQGYAGSTA LGDSMEGLKI EIGGAKTVDQ
AAVVICNALS RKIASHLSVS VENINPSNPV SEYGVDSHVA VELRNWISRS MDCTIPILEI
LAMSMLELSH RIASKRFEGK SE
//
