PKS1_DICDI
ID PKS1_DICDI Reviewed; 3147 AA.
AC Q55E72;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable polyketide synthase 1;
DE Short=dipks1;
DE Includes:
DE RecName: Full=Polyketide synthase stlA;
DE EC=2.3.1.-;
DE Includes:
DE RecName: Full=Chalcone synthase stlA;
DE EC=2.3.1.74;
DE AltName: Full=Steely1;
GN Name=stlA; Synonyms=pks1; ORFNames=DDB_G0269364;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=17660200; DOI=10.1093/bioinformatics/btm381;
RA Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J., Kessin R.H.,
RA Hranueli D.;
RT "Polyketide synthase genes and the natural products potential of
RT Dictyostelium discoideum.";
RL Bioinformatics 23:2543-2549(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2776-3147, FUNCTION, DEVELOPMENTAL
RP STAGE, AND SUBUNIT.
RX PubMed=16906151; DOI=10.1038/nchembio811;
RA Austin M.B., Saito T., Bowman M.E., Haydock S., Kato A., Moore B.S.,
RA Kay R.R., Noel J.P.;
RT "Biosynthesis of Dictyostelium discoideum differentiation-inducing factor
RT by a hybrid type I fatty acid-type III polyketide synthase.";
RL Nat. Chem. Biol. 2:494-502(2006).
CC -!- FUNCTION: Probable polyketide synthase (By similarity). Produces only
CC acylpyrones; in vitro. {ECO:0000250, ECO:0000269|PubMed:16906151}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-
CC tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74;
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16906151}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development. Expressed maximally
CC in early development before cellular aggregation.
CC {ECO:0000269|PubMed:16906151}.
CC -!- DOMAIN: Modular protein possessing six classical catalytic domains and
CC a type III polyketide synthase domain. May facilitate covalent transfer
CC of steely N-terminal acyl products directly to the C-terminal type III
CC PKS active sites, which catalyze both iterative polyketide extension
CC and cyclization.
CC -!- MISCELLANEOUS: In reference to their hybrid nature and to their
CC discovery in D.discoideum, authors term these type I FAS-type III PKS
CC fusion enzymes 'steely'. {ECO:0000305|PubMed:16906151}.
CC -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC synthase genes localized in chromosome 1.
CC -!- SIMILARITY: In the C-terminal section; belongs to the thiolase-like
CC superfamily. Chalcone/stilbene synthases family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72032.1; -; Genomic_DNA.
DR RefSeq; XP_645909.1; XM_640817.1.
DR PDB; 2H84; X-ray; 2.90 A; A/B=2776-3147.
DR PDBsum; 2H84; -.
DR SMR; Q55E72; -.
DR STRING; 44689.DDB0234164; -.
DR PaxDb; Q55E72; -.
DR EnsemblProtists; EAL72032; EAL72032; DDB_G0269364.
DR GeneID; 8616850; -.
DR KEGG; ddi:DDB_G0269364; -.
DR dictyBase; DDB_G0269364; stlA.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q55E72; -.
DR OMA; KMRGGEF; -.
DR PhylomeDB; Q55E72; -.
DR Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-DDI-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00154; -.
DR EvolutionaryTrace; Q55E72; -.
DR PRO; PR:Q55E72; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0102128; F:chalcone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:dictyBase.
DR GO; GO:0030639; P:polyketide biosynthetic process; IDA:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0019505; P:resorcinol metabolic process; IDA:dictyBase.
DR GO; GO:0007165; P:signal transduction; IDA:dictyBase.
DR GO; GO:0048837; P:sorocarp sorus development; IMP:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IGI:dictyBase.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 3.40.50.150; -; 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; IPR012328; Chalcone/stilbene_synt_C.
DR InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF02797; Chal_sti_synt_C; 1.
DR Pfam; PF00195; Chal_sti_synt_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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 3.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Flavonoid biosynthesis; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..3147
FT /note="Probable polyketide synthase 1"
FT /id="PRO_0000377901"
FT DOMAIN 2568..2645
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 161..214
FT /note="Beta-ketoacyl synthase"
FT REGION 345..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..705
FT /note="Acyl/malonyl transferase"
FT REGION 2723..2747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2789..3147
FT /note="Chalcone synthase"
FT ACT_SITE 180
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 682
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2930
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2605
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT STRAND 2788..2795
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 2797..2799
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2803..2813
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2818..2829
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2845..2847
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2849..2854
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2857..2883
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2887..2889
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 2892..2899
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2906..2914
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 2921..2927
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2929..2931
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2932..2944
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 2951..2958
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2961..2963
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 2967..2969
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 2970..2978
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 2982..2991
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 3000..3009
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 3016..3022
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 3025..3030
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 3034..3053
FT /evidence="ECO:0007829|PDB:2H84"
FT TURN 3054..3056
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 3063..3070
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 3075..3084
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 3089..3092
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 3093..3102
FT /evidence="ECO:0007829|PDB:2H84"
FT HELIX 3108..3118
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 3125..3133
FT /evidence="ECO:0007829|PDB:2H84"
FT TURN 3134..3136
FT /evidence="ECO:0007829|PDB:2H84"
FT STRAND 3137..3145
FT /evidence="ECO:0007829|PDB:2H84"
SQ SEQUENCE 3147 AA; 352195 MW; 6B67391AB6596F46 CRC64;
MNKNSKIQSP NSSDVAVIGV GFRFPGNSND PESLWNNLLD GFDAITQVPK ERWATSFREM
GLIKNKFGGF LKDSEWKNFD PLFFGIGPKE APFIDPQQRL LLSIVWESLE DAYIRPDELR
GSNTGVFIGV SNNDYTKLGF QDNYSISPYT MTGSNSSLNS NRISYCFDFR GPSITVDTAC
SSSLVSVNLG VQSIQMGECK IAICGGVNAL FDPSTSVAFS KLGVLSENGR CNSFSDQASG
YVRSEGAGVV VLKSLEQAKL DGDRIYGVIK GVSSNEDGAS NGDKNSLTTP SCEAQSINIS
KAMEKASLSP SDIYYIEAHG TGTPVGDPIE VKALSKIFSN SNNNQLNNFS TDGNDNDDDD
DDNTSPEPLL IGSFKSNIGH LESAAGIASL IKCCLMLKNR MLVPSINCSN LNPSIPFDQY
NISVIREIRQ FPTDKLVNIG INSFGFGGSN CHLIIQEYNN NFKNNSTICN NNNNNNNNID
YLIPISSKTK KSLDKYLILI KTNSNYHKDI SFDDFVKFQI KSKQYNLSNR MTTIANDWNS
FIKGSNEFHN LIESKDGEGG SSSSNRGIDS ANQINTTTTS TINDIEPLLV FVFCGQGPQW
NGMIKTLYNS ENVFKNTVDH VDSILYKYFG YSILNVLSKI DDNDDSINHP IVAQPSLFLL
QIGLVELFKY WGIYPSISVG HSFGEVSSYY LSGIISLETA CKIVYVRSSN QNKTMGSGKM
LVVSMGFKQW NDQFSAEWSD IEIACYNAPD SIVVTGNEER LKELSIKLSD ESNQIFNTFL
RSPCSFHSSH QEVIKGSMFE ELSNLQSTGE TEIPLFSTVT GRQVLSGHVT AQHIYDNVRE
PVLFQKTIES ITSYIKSHYP SNQKVIYVEI APHPTLFSLI KKSIPSSNKN SSSVLCPLNR
KENSNNSYKK FVSQLYFNGV NVDFNFQLNS ICDNVNNDHH LNNVKQNSFK ETTNSLPRYQ
WEQDEYWSEP LISRKNRLEG PTTSLLGHRI IYSFPVFQSV LDLQSDNYKY LLDHLVNGKP
VFPGAGYLDI IIEFFDYQKQ QLNSSDSSNS YIINVDKIQF LNPIHLTENK LQTLQSSFEP
IVTKKSAFSV NFFIKDTVED QSKVKSMSDE TWTNTCKATI SLEQQQPSPS STLTLSKKQD
LQILRNRCDI SKLDKFELYD KISKNLGLQY NSLFQVVDTI ETGKDCSFAT LSLPEDTLFT
TILNPCLLDN CFHGLLTLIN EKGSFVVESI SSVSIYLENI GSFNQTSVGN VQFYLYTTIS
KATSFSSEGT CKLFTKDGSL ILSIGKFIIK STNPKSTKTN ETIESPLDET FSIEWQSKDS
PIPTPQQIQQ QSPLNSNPSF IRSTILKDIQ FEQYCSSIIH KELINHEKYK NQQSFDINSL
ENHLNDDQLM ESLSISKEYL RFFTRIISII KQYPKILNEK ELKELKEIIE LKYPSEVQLL
EFEVIEKVSM IIPKLLFEND KQSSMTLFQD NLLTRFYSNS NSTRFYLERV SEMVLESIRP
IVREKRVFRI LEIGAGTGSL SNVVLTKLNT YLSTLNSNGG SGYNIIIEYT FTDISANFII
GEIQETMCNL YPNVTFKFSV LDLEKEIINS SDFLMGDYDI VLMAYVIHAV SNIKFSIEQL
YKLLSPRGWL LCIEPKSNVV FSDLVFGCFN QWWNYYDDIR TTHCSLSESQ WNQLLLNQSL
NNESSSSSNC YGGFSNVSFI GGEKDVDSHS FILHCQKESI SQMKLATTIN NGLSSGSIVI
VLNSQQLTNM KSYPKVIEYI QEATSLCKTI EIIDSKDVLN STNSVLEKIQ KSLLVFCLLG
YDLLENNYQE QSFEYVKLLN LISTTASSSN DKKPPKVLLI TKQSERISRS FYSRSLIGIS
RTSMNEYPNL SITSIDLDTN DYSLQSLLKP IFSNSKFSDN EFIFKKGLMF VSRIFKNKQL
LESSNAFETD SSNLYCKASS DLSYKYAIKQ SMLTENQIEI KVECVGINFK DNLFYKGLLP
QEIFRMGDIY NPPYGLECSG VITRIGSNVT EYSVGQNVFG FARHSLGSHV VTNKDLVILK
PDTISFSEAA SIPVVYCTAW YSLFNIGQLS NEESILIHSA TGGVGLASLN LLKMKNQQQQ
PLTNVYATVG SNEKKKFLID NFNNLFKEDG ENIFSTRDKE YSNQLESKID VILNTLSGEF
VESNFKSLRS FGRLIDLSAT HVYANQQIGL GNFKFDHLYS AVDLERLIDE KPKLLQSILQ
RITNSIVNGS LEKIPITIFP STETKDAIEL LSKRSHIGKV VVDCTDISKC NPVGDVITNF
SMRLPKPNYQ LNLNSTLLIT GQSGLSIPLL NWLLSKSGGN VKNVVIISKS TMKWKLQTMI
SHFVSGFGIH FNYVQVDISN YDALSEAIKQ LPSDLPPITS VFHLAAIYND VPMDQVTMST
VESVHNPKVL GAVNLHRISV SFGWKLNHFV LFSSITAITG YPDQSIYNSA NSILDALSNF
RRFMGLPSFS INLGPMKDEG KVSTNKSIKK LFKSRGLPSL SLNKLFGLLE VVINNPSNHV
IPSQLICSPI DFKTYIESFS TMRPKLLHLQ PTISKQQSSI INDSTKASSN ISLQDKITSK
VSDLLSIPIS KINFDHPLKH YGLDSLLTVQ FKSWIDKEFE KNLFTHIQLA TISINSFLEK
VNGLSTNNNN NNNSNVKSSP SIVKEEIVTL DKDQQPLLLK EHQHIIISPD IRINKPKRES
LIRTPILNKF NQITESIITP STPSLSQSDV LKTPPIKSLN NTKNSSLINT PPIQSVQQHQ
KQQQKVQVIQ QQQQPLSRLS YKSNNNSFVL GIGISVPGEP ISQQSLKDSI SNDFSDKAET
NEKVKRIFEQ SQIKTRHLVR DYTKPENSIK FRHLETITDV NNQFKKVVPD LAQQACLRAL
KDWGGDKGDI THIVSVTSTG IIIPDVNFKL IDLLGLNKDV ERVSLNLMGC LAGLSSLRTA
ASLAKASPRN RILVVCTEVC SLHFSNTDGG DQMVASSIFA DGSAAYIIGC NPRIEETPLY
EVMCSINRSF PNTENAMVWD LEKEGWNLGL DASIPIVIGS GIEAFVDTLL DKAKLQTSTA
ISAKDCEFLI HTGGKSILMN IENSLGIDPK QTKNTWDVYH AYGNMSSASV IFVMDHARKS
KSLPTYSISL AFGPGLAFEG CFLKNVV
