GRA1_CLAGR
ID GRA1_CLAGR Reviewed; 2089 AA.
AC E9KMQ2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Non-reducing polyketide synthase PKS16 {ECO:0000303|PubMed:21289108};
DE Short=NR-PKS PKS16 {ECO:0000303|PubMed:21289108};
DE EC=2.3.1.- {ECO:0000305|PubMed:21289108};
DE AltName: Full=Grayanic acid biosynthesis cluster PKS {ECO:0000303|PubMed:21289108};
GN Name=PKS16 {ECO:0000303|PubMed:21289108};
OS Cladonia grayi (Gray's cup lichen).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Cladoniaceae;
OC Cladonia.
OX NCBI_TaxID=27339;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND FUNCTION.
RX PubMed=21289108; DOI=10.3852/10-335;
RA Armaleo D., Sun X., Culberson C.;
RT "Insights from the first putative biosynthetic gene cluster for a lichen
RT depside and depsidone.";
RL Mycologia 103:741-754(2011).
RN [2]
RP FUNCTION.
RX DOI=10.1016/0147-5975(92)90041-O;
RA Culberson C., Armaleo D.;
RT "Induction of a complete secondary-product pathway in a cultured lichen
RT fungus.";
RL Exp. Mycol. 16:52-63(1992).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of orcinol depsidone grayanic acid
CC (GRA), the only major secondary metabolite known in C.grayi
CC (PubMed:21289108). The first step consists in the ring and depside
CC synthesis by PKS16 leading to 4-O-demethylsphaerophorin, involving
CC different orcinol-like rings, one with acetyl CoA and the other with
CC octanoyl CoA as the starter (Probable). Further depsidone formation by
CC the GRA cluster-specific cytochrome P450 leads to 4-O-demethylgrayanic
CC acid (Probable). Finally, the cluster specific O-methyltransferase
CC probably converts the 4-O-demethylgrayanic acid into grayanic acid
CC (Probable). {ECO:0000269|PubMed:21289108, ECO:0000305|PubMed:21289108,
CC ECO:0000305|Ref.2}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:21289108}.
CC -!- INDUCTION: Expression is induced during grayanic acid production
CC conditions. {ECO:0000269|PubMed:21289108}.
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 an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5B0D0,
CC ECO:0000305|PubMed:21289108}.
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DR EMBL; GU930713; ADM79459.1; -; Genomic_DNA.
DR AlphaFoldDB; E9KMQ2; -.
DR SMR; E9KMQ2; -.
DR BioCyc; MetaCyc:MON-21839; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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; 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; 2.
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.
PE 2: Evidence at transcript level;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat;
KW Transferase.
FT CHAIN 1..2089
FT /note="Non-reducing polyketide synthase PKS16"
FT /id="PRO_0000445362"
FT DOMAIN 1617..1694
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1729..1806
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..243
FT /note="N-terminal acylcarrier protein transacylase (SAT)
FT domain (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21289108"
FT REGION 342..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..796
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21289108"
FT REGION 891..1214
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21289108"
FT REGION 1273..1586
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21289108"
FT REGION 1697..1730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..2083
FT /note="Thioesterase (TE) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:21289108"
FT COMPBIAS 1715..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1654
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1766
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2089 AA; 227870 MW; F19F2C290E42A140 CRC64;
MTLPNNVVLF GDQTVDPCPI IKQLYRQSRD SLTLQTLFRQ SYDAVRREIA TSEASDRALF
PSFDSFQDLA EKQNERHNEA VSTVLLCIAQ LGLLMIHVDQ DDSTFDARPS RTYLVGLCTG
MLPAAALAAS SSTSQLLRLA PEIVLVALRL GLEANRRSAQ IEASTESWAS VVPGMAPQEQ
QEALAQFNDE FMIPTSKQAY ISAESDSSAT LSGPPSTLLS LFSSSDIFKK ARRIKLPITA
AFHAPHLRVP DVEKILGSLS HSDEYPLRND VVIVSTRSGK PITAQSLGDA LQHIIMDILR
EPMRWSRVVE EMINGLKDQG AILTSAGPVR AADSLRQRMA SAGIEVSRST EMQPRQEQRT
KPRSSDIAII GYAARLPESE TLEEVWKILE DGRDVHKKIP SDRFDVDTHC DPSGKIKNTS
YTPYGCFLDR PGFFDARLFN MSPREASQTD PAQRLLLLTT YEALEMAGYT PDGTPSTAGD
RIGTFFGQTL DDYREANASQ NIEMYYVSGG IRAFGPGRLN YHFKWEGPSY CVDAACSSST
LSIQMAMSSL RAHECDTAVA GGTNVLTGVD MFSGLSRGSF LSPTGSCKTF DNDADGYCRG
DGVGSVILKR LDDAIADGDN IQAVIKSAAT NHSAHAVSIT HPHAGAQQNL MRQVLREGDV
EPADIDYVEM HGTGTQAGDA TEFASVTNVI TGRTRDNPLH VGAVKANFGH AEAAAGTNSL
VKVLMMMRKN AIPPHIGIKG RINEKFPPLD KINVRINRTM TPFVARAGGD GKRRVLLNNF
NATGGNTSLL IEDAPKTDIQ GHDLRSAHVV AISAKTPYSF RQNTQRLLEY LQLNPETQLQ
DLSYTTTARR MHHVIRKAYA VQSIEQLVQS LKKDISSSSE PGATTEHSSA VFLFTGQGSQ
YLGMGRQLYQ TNKAFRKSIS ESDSICIRQG LPSFEWIVSA EPSEERITSP SESQLALVAI
ALALASLWQS WGITPKAVMG HSLGEYAALC VAGVLSISDT LYLVGKRAQM MEKKCIANTH
SMLAIQSDSE SIQQIISGGQ MPSCEIACLN GPSNTVVSGS LTDIHSLEEK LNAMGTKTTL
LKLPFAFHSV QMDPILEDIR ALAQNVQFRK PIVPIASTLL GTLVKDHGII TADYLTRQAR
QAVRFQEALQ ACRAENIATD DTLWVEVGAH PLCHGMVRST LGLSPTKALP SLKRDEDCWS
TISRSIANAY NSGVKVSWID YHRDFQGALR LLELPSYAFD LKNYWIQHEG DWSLRKGETT
RTTAPPPQAS FSTTCLQVIE NETFTQDSAS VTFSSQLSEP KLNTAVRGHL VSGTGLCPSS
VYADVAFTAA WYIASRMTPS DPVPAMDLSS MEVFRPLIVD SNETSQLLRV SATRNPNEQI
VNIKISSQDD KGRQEHAHCT VMYGDGHQWM EEWQRNAYLI QSRIDKLTQP SSPGIHRMLK
EMIYKQFQTV VTYSPEYHNI DEIFMDCDLN ETAANIKLQS TAGHGEFIYS PYWIDTVAHL
AGFILNANVK TPADTVFISH GWQSFQIAAP LSAEKTYRGY VRMQPSSGRG VMAGDVYIFD
GDEIVVVCKG IKFQQMKRTT LQSLLGVSPA ATPTSKSIAA KSTRPQLVTV RKAAVTQSPV
AGFSKVLDTI ASEVGVDVSE LSDDVKISDV GVDSLLTISI LGRLRPETGL DLSSSLFIEH
PTIAELRAFF LDKMDMPQAT ANDDDSDDSS DDEGPGFSRS QSNSTISTPE EPDVVNVLMS
IIAREVGIQE SEIQLSTPFA EIGVDSLLTI SILDALKTEI GMNLSANFFH DHPTFADVQK
ALGAAPTPQK PLDLPLARLE QSPRPSSQAL RAKSVLLQGR PEKGKPALFL LPDGAGSLFS
YISLPSLPSG LPIYGLDSPF HNNPSEFTIS FSDVATIYIA AIRAIQPKGP YMLGGWSLGG
IHAYETARQL IEQGETISNL IMIDSPCPGT LPPLPAPTLS LLEKAGIFDG LSTSGAPITE
RTRLHFLGCV RALENYTVTP LPPGKSPGKV TVIWAQDGVL EGREEQGKEY MAATSSGDLN
KDMDKAKEWL TGKRTSFGPS GWDKLTGTEV HCHVVGGNHF SIMFPPKVC
