MELA_PENEN
ID MELA_PENEN Reviewed; 2138 AA.
AC A0A0A2KT65;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Conidial yellow pigment biosynthesis polyketide synthase melA {ECO:0000303|PubMed:35339702};
DE Short=PKS melA {ECO:0000303|PubMed:35339702};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q03149};
GN Name=melA {ECO:0000303|PubMed:35339702}; ORFNames=PEX2_000770;
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8;
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).
RN [2]
RP IDENTIFICATION, FUNCTION, AND INDUCTION.
RX PubMed=35339702; DOI=10.1016/j.fgb.2022.103689;
RA Clemmensen S.E., Kromphardt K.J.K., Frandsen R.J.N.;
RT "Marker-free CRISPR-Cas9 based genetic engineering of the phytopathogenic
RT fungus, Penicillium expansum.";
RL Fungal Genet. Biol. 160:103689-103689(2022).
CC -!- FUNCTION: Non-reducing polyketide synthase involved in the biosynthesis
CC of a yellow conidial pigment (PubMed:35339702). Probably forms the
CC heptaketide naphthopyrene YWA1 via condensation of acetate units (By
CC similarity). {ECO:0000250|UniProtKB:Q03149,
CC ECO:0000269|PubMed:35339702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O +
CC YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:133763;
CC Evidence={ECO:0000250|UniProtKB:Q03149};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC Evidence={ECO:0000250|UniProtKB:Q03149};
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:35339702}.
CC -!- PATHWAY: Polyketide biosynthesis; heptaketide naphthopyrone YWA1
CC biosynthesis. {ECO:0000250|UniProtKB:Q03149}.
CC -!- INDUCTION: Expression is limited to the conidia.
CC {ECO:0000269|PubMed:35339702}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and 2 acyl-carrier protein (ACP) domains
CC that serve as the tethers of the growing and completed polyketide via
CC their phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The C-terminal region is involved in Claisen-type cyclization
CC of the second ring of naphthopyrone. {ECO:0000250|UniProtKB:Q03149}.
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DR EMBL; JQFZ01000147; KGO57402.1; -; Genomic_DNA.
DR RefSeq; XP_016599070.1; XM_016737355.1.
DR STRING; 27334.A0A0A2KT65; -.
DR EnsemblFungi; KGO43372; KGO43372; PEXP_096630.
DR EnsemblFungi; KGO57402; KGO57402; PEX2_000770.
DR EnsemblFungi; KGO71027; KGO71027; PEX1_071910.
DR GeneID; 27672774; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OrthoDB; 68112at2759; -.
DR PhylomeDB; A0A0A2KT65; -.
DR UniPathway; UPA00167; -.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..2138
FT /note="Conidial yellow pigment biosynthesis polyketide
FT synthase melA"
FT /id="PRO_0000456062"
FT DOMAIN 1640..1714
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1759..1836
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..244
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 376..807
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 910..1229
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1288..1601
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1863..2135
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT ACT_SITE 545
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 999
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1953
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1674
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1796
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2138 AA; 233216 MW; AB8CDBC8024D4FD4 CRC64;
MEGPSHVYLF GDQTADFDSG LRRLLHAKND SLLAAFFQKS YYALRKEITS LPPSERQGFP
RFTSIVDLLA RFKESGPNPA LESALTTIHQ LGCFIHYYGD LGHAYPSADE SCIIGLCTGQ
LASAAVSSSR TIGELISAGI ETVVLALRLG MCVLKVQELI EPSKSATPSW SVLISGMHEP
EAENLIQQYA KKNALPRVSQ PYISAVSPNG LTISGPPTFL SRFIEDSVSK EHKPTRVPIH
GPYHASHLYD DRDINRILES WPTEQFMTFV PQIPVISSET GKEFQAESLE QLLRLSLQEI
LQRQLCWDKV IESCQETLEL ATTCTLFPIS STATQSLFNS LKKAGVSNLE VDSTIGDVQK
DSEGDNRTGR AEQSKIAIIG LSGRFPESPD TEAFWDLLKK GLDVHREVPP ERWDVKAHVD
KDGKIRNTSQ VQYGCWYNDA GMFDPRFFNM SPREALQADP AQRLALLTAY EALEMAGFIP
DSTPSTQKNR VGVFYGMTSD DYREVNSGQD IDTYFIPGGN RAFTPGRINY YFKFSGPSVS
VDTACSSSLA AIHVACNSLW RNECDSAVAG GVNILTNPDN HAGLDRGHFL SRTGNCTTFD
DGADGYCRAD GIGSIVIKRL EDAQADNDPI YGIIGGAYTN HSAEAVSITR PHVGAQSFIF
DKLLNESNSD PKEISYIEMH GTGTQAGDAV EMQSVLDVFA PDYRRGPAQS LHLGSAKSNV
GHGESASGVT ALIKVLMMMQ KNMIPPHCGI KTKINHNFPT DFPQRNVHIA SEPTPWNRPN
GGKRKTFVNN FSAAGGNTAL MVEDGPLDEE NVEDPRSAHP VLVSARSQSA LKNNISALVQ
YIDKNKNLFN SNEASLLANL SYTTTARRIH HPFRVAVTGS TLDEVRSGLA PIVNRDSISP
APANAPGIGF VFTGQGAQYT GMGRQLFESC SQFRAHIEHL NCIGQSQGFP SILSLVDGSV
PIEEHSPVVT QLGTTCVQMA LTKYWMSLGI SPAFVIGHSL GEFAALNASG VLTTSDTIYL
AGRRAQLLTE QIKVGTHAML AVKSSVAQVK QFLDDATEVA CINAPSETVI SGAREKIDEL
AQTLTNEGFK ATKLNVPFAF HSAQVEPILE SLSEIGKGVN FNAPSIPFVS ALLGDVINES
NSELLGPNYL TRHCRETVNF LGALEATRHS NLMNDKTIWI EIGSHPVCSG MVKATFGPQA
TTVASLRRQE DTWKVLSASV SALYMAGIEL RWKEYHQDFT AGHKVLPLPS YKWDLKNYWI
PYTNNFCLLK GAPAVPVAEA APVAVFLSSA AQRVLETSGD NSSASIVIEN DIADPELNRV
IAGHKVNGAC LTPSSLYADI AQTLGEYLVQ NYKPEWKDRG FDICNMMVPK PLIAKGGKQL
FRVSATANWA EESAKVQVWS VTPEGKKILD HASCNIKFFD PSPYELEWKR SSYLIKRSIE
HLQESTISGQ AHRMKRGMVY KLFASLVDYD DNYKSMREVI LDSEQHEATA VVKFEAPPGN
FHRNPFWIDS IGHLSGFIMN ASDNTDSKNQ VFVNHGWDSM RCLKKFDPSV TYRTYVRMQP
WKDSIWAGDV YMFDGDDVVA VYGGVKFQGL ARKILDMALP PGGASAPKPA AKRVPAPINV
QKAKPSVTKK ASPSPKSGLP SMATRALAIL AEEVGLAASE MTDDLNFADY GVDSLLSLTV
TGRYREDMGL DLDSTVFVDS PTVKDFKHLL AQMGPGESSD GSSSEGDMSS AASSTDLSSP
NTSGLPTPAN EKSMTHGLQG QNDSMRQIAS ILAEEIGVDS EELLGDANLG EMGLDSLMSL
TVLGKIREDL DLDLPGEFFI ENQTLDDIET TLDLKPKLAP AEPIRLPEQI PVEAPVVAHS
TATQHPPATS ILLQGNPKTA TQSLFLFPDG SGSATSYATI PGISPDVCVY GLNCPYMRTP
ENLKFSLDEL TAPYVAEIRR RQPTGPYNFG GWSAGGICAY DAARKLIFEE GERVERLLLL
DSPFPIGLEK LPPRLYSFFD TIGLFGEGKA PPPKWLLPHF LAFIDSLDAY KAVPFPYEDP
KHADKLPKTF MVWAKDGVCS KPGDARPAPA ADGSADPREM LWLLNNRTDL GPNGWDTLVG
PKHVGGITVM EDANHFTMTR GQKAKELARF IANSMASA
