ID A0A0A2KMX0_PENIT Unreviewed; 2501 AA.
AC A0A0A2KMX0;
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:KGO68231.1};
GN ORFNames=PITC_046570 {ECO:0000313|EMBL:KGO68231.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO68231.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO68231.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO68231.1,
RC ECO:0000313|Proteomes:UP000030104};
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:KGO68231.1}.
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DR EMBL; JQGA01001217; KGO68231.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2KMX0; -.
DR HOGENOM; CLU_000022_31_1_1; -.
DR OMA; EDVGWIS; -.
DR OrthoDB; 5396558at2759; -.
DR PhylomeDB; A0A0A2KMX0; -.
DR Proteomes; UP000030104; 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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 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; 1.
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; IPR013149; ADH-like_C.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF28; SYNTHASE, PUTATIVE-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Hydrolase {ECO:0000313|EMBL:KGO68231.1};
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:UP000030104};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO68231.1}.
FT DOMAIN 65..488
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2413..2489
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2501 AA; 274678 MW; 35946DBBEFEDA419 CRC64;
MAPFINNTNK SNSYLLNTDG FDNGANEHLD DPSGTNSMPS STTWAGTTRD SSPPEESHAS
KAPSQEPIAI CGMSVRLPGG LHSPQQLWDF LIAKGDASGP VPKSRYNASG YYSEMPKPGS
VKTERGYFLD ESIDLASIDT SFFSMAKVDV ERMDPHQRQM LEVARECIED AGVTNWKGRP
IGCYMGSFGE DWAEIFAKED QQYGLYRVTG YGDFMLSNRI SYEMDLTGPS MVIRTGCSAA
LVALHEACLA VSRGDCEGAI VGGANLIMAP GMTIAMTEQG VLSPDGSCKT FSADANGYAR
GEAVSAIFIK PLSDAIRDGN PVRAVIRATA SNSDGKGSGG GLQMPNDVAQ EAMIRRAYEI
AGIPDYSETA FVECHGTGTA IGDPIETRAV GRVFGPSGGV HIGSVKPNLG HSEGASGLTS
LIKSVLALEH RIIPPNIKFN EPNPSIPWDS CGLSVPTEAM PWPKSRSERI SVNSFGIGGT
NAHVILDSAQ SFGVSPIPDR PTTSPQLLIY SANNAESLKK MTVSCKDYIQ KHPGKVDHLA
FTLANRREHL PHRAFAVANM IGEVTASIPF RSGETPNIVM VFTGQGAQWP EMGRCMILSS
AYPIFKKSIK SLDAHIRNLK DSPEWTIEEE LQKPTKTSRL DSAEFSQPLC TAIQIALVDT
FASVGIQPTA VVGHSSGEIA AAYAAGAITA KEAITIAFYR GQVTKLQTKA GAMASIGLGS
RSVQEFLQPG VTVACENSNK SVTLAGDCEA VELVMIRIKE AHPHVLARKL QVDKAYHSHH
MAEIGDKYHA FIENHISSKS PERTIEKLFF SSVEGKLITQ ESNLESRYWQ RNLESPVLFH
SAISSIIQHD IAKNMVFLEV GPHSALAGPL RQIQTHLSNT SPYASALIRN LNDVESFLTA
VGKLYALNAS LDFSRVIPEG SVLPDLPRYH WDHSKKFWHE SRLSKNWRHR EHKYHDLLGV
RVAESLEFEV LFRNLFHLEN AAWIRDHKVG EDTVFPFAAY AGMVGEAVRQ VTGVNEAFQM
RNVVVSTALV LRESEPVELM TTMRRRRLTD SLDSDWWEFI IASHTGTVST KHCFGEVRAH
SENVCRAEST VPLVRKIDTR RCYRSMARCG LNFGPAFQRL DDIRSDTLTR MATSEVIGRA
TDGEGYHLHP TIIDASLQLL TVAASKGYAD PTTKMMVPTN IEELCIYRCH GDVQVRASAS
YTPNGSIIGG GKCISSNGKL VLHGSGIRLS VLDEQASGKV DETTARAEWG PHIDFMDVNT
LIQPSIDRSA HTRAVTELFH MCMLHTKRVI AGLDTPLSHM QKYRSWIDQQ LQLCEFEHLQ
SLDNPALEEQ IKRIVHDLSQ TIADVPSKAI QKIFSNVKGI FTGEVDALDL LLSDGTLNSL
YALIDQCDES QFFEHLAHCK PNLRILEIGA GLGGSTANVL RLLTPGGRTL YSSYTFTDIS
SGFFVAAKDR FSSYPNIEYA TLDISKNCSE QGFDGCTYDL ILATNVLHVT PSLNVSLNNV
RKLLAPSGRL LLHELTPTSK WVNYIWGTLP GWWQGEADGR VDEPYVGVHR WKKELMAAGF
RTPDAVVLDS PEPYQLGAVI VARSNLEIVP EKRVTLLSLS ESTRVRSMVQ ALENRGYVVD
YRGLQDLPLP ASQDVIAFLD DEAPFFENMD HQRFESFKDL VENMKDCGIL WVTGLLQIEC
RDPRFGQING IARSIRSERL VDFATCEVDN VDSSIEKIID VFKSFQLRQE AHALKPELEY
AIVKNAVQVS RVHPFAVQEE LLTSDASDVI ALRTSKPGRL SALHWARQGI ESLEGDDVEI
NTYSTGLNFK DVLCAMGIVE ASEVGFGLEA AGIVRRTGPH VKDLKEGDRV MLMGSCSFST
QVVVSENLCE KIPGGLSFED AATMPCVFAT AMYCIFNVGN LQKGQSILIH SACGGVGLAT
IQLAQMIGAE IYATVGNDQK VKYLMDTFGI PRNRIFNSRD TSFTEHVLRE TNGEGVDLAL
NSLSGELLHA TWKCIAAFGK MVEIGKRDLI GSGKLDMSPF IENRSYCCVD LDQICSKKPI
IVKQLLKSVV RLLRDRYIHP IRPIKVFKAD EILDAFRYMQ QGIHLGKIVV SIRDSAGQVS
IVSNVQKRRE PTEFPSSGAY LLVGGLGGLG RSLSVWMVER GARHLIYLSP SAGTKQEHLE
FARELASMGC RADFVQGTVL NLDDVNKSIK QAQGQLKGIF QMSMVNRDQN LTRMTLEDWN
VAVDPKVNGT WNLHNAAVSA DAELDFFVLF SSLSGMFGQP GQSNYAGANT FLDAFSQYRL
SLGLPACAIA IGAVEEVGCL AVRESIMQRF KATGIMGDTI SVCELFEGME LAIKSTTNKS
NPFTSNNFCI GLRSRVPISD PGNRALWKKD MRTAVFHNKG ATGNKSSTST SDGLRSFISS
AKSNPALLAQ PDSAHFLAVE IGKKVFSFLL KSEEDLHTWC SLSDLGMDSL VAIEVRQWWK
MTFEFDISVL EMMGMSTLDV LGEHAARGML KLFHGVEKED N
//