PGMA_ASPTN
ID PGMA_ASPTN Reviewed; 2298 AA.
AC A0A1W7M1U5; Q0CJC8;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Non-reducing polyketide synthase pgmA {ECO:0000303|PubMed:28471414};
DE Short=NR-PKS pgmA {ECO:0000303|PubMed:28471414};
DE EC=2.3.1.- {ECO:0000269|PubMed:35351612};
DE AltName: Full=Pigmented naphthoquinones biosynthesis cluster protein A {ECO:0000303|PubMed:28471414};
GN Name=pgmA {ECO:0000303|PubMed:28471414}; ORFNames=ATEG_06206;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND IDENTIFICATION.
RC STRAIN=NIH 2624 / FGSC A1156;
RX PubMed=28471414; DOI=10.3390/microorganisms5020022;
RA Palonen E.K., Raina S., Brandt A., Meriluoto J., Keshavarz T., Soini J.T.;
RT "Melanisation of Aspergillus terreus-is butyrolactone I involved in the
RT regulation of both DOPA and DHN types of pigments in submerged culture?";
RL Microorganisms 5:0-0(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DOMAIN, DISRUPTION PHENOTYPE, INDUCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=35351612; DOI=10.1016/j.fgb.2022.103690;
RA Tang S., Men P., Zhang W., Li H., Li Z., Huang X., Lu X.;
RT "Identification of a polyketide biosynthesis gene cluster by
RT transcriptional regulator activation in Aspergillus terreus.";
RL Fungal Genet. Biol. 160:103690-103690(2022).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of pleosporalin A, ascomycone A, as well
CC as a third cryptic naphthoquinone derived pigment, all responsible for
CC the coloration of conidia (PubMed:28471414, PubMed:35351612). The non-
CC reducing polyketide synthase pgmA is responsible for the condensation
CC of seven acetyl-CoA units to produce the cyclized heptaketide 3-
CC acetonyl-1,6,8-trihydroxy-2-naphthaldehyde (PubMed:35351612). The
CC pathway begins with the biosynthesis of the cyclized heptaketide 3-
CC acetonyl-1,6,8-trihydroxy-2-naphthaldehyde by the NR-PKS pgmA. The C-6
CC hydroxyl group is further methylated by the O-methyltransferase pgmB to
CC yield fusarubinaldehyde which is in turn oxidized by the cytochrome
CC P450 monooxygenase pgmC at C-9. The C-1 hydroxyl group is then
CC methylated spontaneously. Although pgmE, pgmD and pgmH are essential
CC for the production of pleosporalin A, it is not the case for the 2
CC other final products and it remains difficult to assign a specific
CC function to each enzyme. PgmF and pgmG seem not to be involved in
CC pigment biosynthesis although they were regulated by the cluster-
CC specific transcription factor pgmR (PubMed:35351612) (Probable).
CC {ECO:0000269|PubMed:28471414, ECO:0000269|PubMed:35351612,
CC ECO:0000305|PubMed:35351612}.
CC -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:35351612}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:35351612}.
CC -!- INDUCTION: Expression is positively regulated by the pgm cluster-
CC specific transcription factor pgmR. {ECO:0000269|PubMed:35351612}.
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 back-
CC bone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers
CC the extender unit malonyl-CoA; a product template (PT) domain that
CC controls the immediate cyclization regioselectivity of the reactive
CC polyketide backbone; and 2 acyl-carrier protein (ACP) that serve as the
CC tethers of the growing and complete polyketide via their
CC phosphopantetheinyl arm. At the C-terminus, FSR1 exhibits a reductase
CC (R) domain instead of the canonical TE domain. In contrast to TE and
CC TE/CLC domains, R domains show sequence similarities to the short-chain
CC dehydrogenase/reductase (SDR) superfamily, exhibiting Rossman fold
CC structure and nucleotide binding motifs. {ECO:0000305|PubMed:28471414}.
CC -!- DISRUPTION PHENOTYPE: Abolished completely the production of the
CC naphthoquinones derived pigments. {ECO:0000269|PubMed:35351612}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU33967.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BK009975; DAA80467.1; -; Genomic_DNA.
DR EMBL; CH476601; EAU33967.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215384.1; XM_001215384.1.
DR EnsemblFungi; EAU33967; EAU33967; ATEG_06206.
DR GeneID; 4321475; -.
DR VEuPathDB; FungiDB:ATEG_06206; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_16_6_1; -.
DR OMA; CMDITEM; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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 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; IPR013120; Far_NAD-bd.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2298
FT /note="Non-reducing polyketide synthase pgmA"
FT /id="PRO_0000456001"
FT DOMAIN 1641..1716
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1765..1840
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..333
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28471414"
FT REGION 361..732
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28471414"
FT REGION 901..1193
FT /note="Acyl/malonyl transferases"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28471414"
FT REGION 1294..1586
FT /note="Product template (PT) domainn"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28471414"
FT REGION 1927..2178
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:28471414"
FT ACT_SITE 532
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 994
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1675
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1799
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2298 AA; 252618 MW; C329302811D800A9 CRC64;
MPNTTMELFI FGDQTLDVQP CLRGLAQHRH NPVLEDFFTK TYQVLRTEID QLPHNVKVGL
PRFTCIDDII FRPPGSKSCI ALDMAMTTFY QLGVFIRVTC ALGLCTGALA AAAVSCSRNA
LDLVPMAVDA VRVAFRTGAH VLDIAHRIES PDASDQSWLL YVPAVEAAET ALKAFREHTL
LPGIRQPYIT AYTLNSVMVS GPPSSLEQLK RHAPFRELNP QSVSINGPYH APHLYSQEDI
DDIVGDLACQ DVHSCSCRVP VIAGDGNPVP DADFGTILKA AVAQILRQQI NWNGILRELL
TRHDIAGSLT LTVTTIGTKT DHFIYNVLKQ SPLREYLSSK PAQSRQPVSN EGAPEPGNGR
QKLAIIGMSG RFPGADDIEE FWTLLEQGLD VHKPVPSLRW DAQTHVDPTR ARKNTSSTPF
GCWLEHPDLF DARFFNISPR EAPQIDPAQR LALMTAYEAI EQAGIVPDAT PSTRRDRVGV
FYGTTSNDWM ETNSAQNIDT YFIPGGNRAF IPGRINYYFK FSGPSYAVDT ACSSSLASIH
LACNALWRRE IDTAIAGGTN VLTNPDFTAG LDRGQFLSRT GNCKTFDDSA DGYCRGEGVA
TVIIKRLEDA VADKDPILGL ILSASTNHSA ESESITRPHV GAQREILSNI LNRGASNPYD
VSYVEMHGTG TQVGDASEMS SVLETFAPAP NRVKSARGHD TPLYLGSAKA NIGHGEAVSG
VSSLIKVLLM MQRNTIVPHC GIKTKINHKF PTDLKDRNAH IALQPVSWER NSASSQTRKV
VVNNFSAAGG NSALLVEDAP PKRESPGEAA LVDPRQHHVV AVSARNAVSL EGNIRSMLKY
LRENPDVQLG KLSYTTTARR LHHQHRVMVT GSKVEDIATQ LQAALDEKTG MTRPKAALKV
VFAFTGQGAH YPGMGKELFE NFSVFRTEVH RLDRLGQTMG FPSVLPVIQS PANDIDIGTF
QPSAVQLAGV CTQMALCKLW AAWNITPTAV VGHSLGEYPA LNAAGVLSDA DTIYLVGKRA
QLLEEKCVRG THSMLAIKAS VDQITGALEN MKYHVACINS PVETVLAAAN EELYALKDVL
TAAGFKSTPL KVPYAFHSPQ VDPVLADFKE LSRGVTFSRP RIPILSALDG NLHVDDHFFD
PEYLIRHTRE PVNMHRTLLT AAREHVITEM TTVLEIGSHP AVSGMVKGVL GPQVSCLATA
SRGRPNLQVL AATLKVLYMK GADICWPQYH IDFKASHEVI PLPAYSWDLK SYWIQYVNDW
SLRKGDPPQV IQSSPALEST TVHRVVEETH DSTKTRIVIE ADIARKDLSP LVQGHEVDGI
PLCTPSVYAD MALTLGTYLL KRYRPDQNDS LVDVTDMVIS KALILRAGAS EQLLQAHADA
DWAANAVTIK FKSFDARQKL QEHSQCVVRF RDRGLLEDLQ NSAPSVKAKT QALRDGIVTG
ETARFNRPMV YRAIRPLAKF HEDYRAIDEI VLNSETLEAS SRLSFGDVKR GGTYHTHPAI
IDSLTQSCGF TMNCNDRSDL DKEVFMNHGW GSLQIFEPLS FDKVYTTYTR MAEGSDHLWH
GDVVIFDGDK VVAYIGQISI QGVPRRVLKT VLSIESGSQK KHQPTQMKQP HTATQANGYP
VANGHAQATP TSGPVNGEPR PSRFPRALEI IAEESGLSLA DLTDTTVFSD VGIDSLLNLT
ISSRFKEEFD VDLDFTALSQ DYPTVASLRA LLSEPERSTN GMPAASAKDT SRFDEIPPMN
GHKTNGHVMN GHSNGSSNGL PDTDKVDFQR VLQIISEESG VAMEELSEDT NFADAGIDSL
LSLVIVSRFR DELELDIAHE SLLMDCQSVA DLKRYLFPQD HSTAENGVEP PAKNGLAADA
PAVSSMSQDI ISNGNGETAQ PLGASLLLRQ KAVDHYVQKY TAGFNAPIPN GAGNESEKTD
NVKVVLVTGA SGSLGGHLID QLAQRADVKT VVCLNREHNL EPYTRQQKAM RDKGIRSFDK
IRSKLLVLQT DSSQPMLGLP KSQYEELVDS VTHVIHNAWP MSAKRPLDGF EKQFQILRNL
IDFACVVTSR RPKSFKFGFQ LVSSIGVVGH HGLSKPHDRK EKTIVPESRV NIDSVLPNGY
SEAKWACERM LDETLHKHYA DRVRTMVVRL GQIAGSKRCG YWNPTEHFGF LIKSSQTLNA
LPDVPGMVYW TPVEEVAGSL VDLILADNRP YPVYHVDNPI GQPWSEMNKV LADALNIPNL
VPFVEWVERV RSAPHRDNPA AMLSDFFIDN YLRMSCGGLV LDVKNTLEHS RVLSGVGPVT
EDVVRKYIHV WKEIGFLK
