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Database: UniProt
Entry: A0A0A2KMX0_PENIT
LinkDB: A0A0A2KMX0_PENIT
Original site: A0A0A2KMX0_PENIT 
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
//
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