STLB_DICDI
ID STLB_DICDI Reviewed; 2968 AA.
AC Q54FI3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Polyketide synthase 37 {ECO:0000303|PubMed:16906151};
DE Short=dipks37 {ECO:0000303|PubMed:16906151};
DE Includes:
DE RecName: Full=Highly reducing polyketide synthase StlB {ECO:0000303|PubMed:16906151};
DE EC=2.3.1.- {ECO:0000269|PubMed:16906151};
DE Includes:
DE RecName: Full=Chalcone synthase {ECO:0000303|PubMed:16906151};
DE EC=2.3.1.74 {ECO:0000269|PubMed:16906151};
DE AltName: Full=Steely2 {ECO:0000303|PubMed:16906151};
GN Name=StlB; Synonyms=pks37; ORFNames=DDB_G0290853;
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 FUNCTION.
RX PubMed=9446571; DOI=10.1074/jbc.273.5.2669;
RA Kay R.R.;
RT "The biosynthesis of differentiation-inducing factor, a chlorinated signal
RT molecule regulating Dictyostelium development.";
RL J. Biol. Chem. 273:2669-2675(1998).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=20231486; DOI=10.1073/pnas.1001681107;
RA Neumann C.S., Walsh C.T., Kay R.R.;
RT "A flavin-dependent halogenase catalyzes the chlorination step in the
RT biosynthesis of Dictyostelium differentiation-inducing factor 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5798-5803(2010).
CC -!- FUNCTION: Polyketide synthase; part of the gene cluster that mediates
CC the biosynthesis of DIF-1 (Differentiation Inducing Factor-1), a signal
CC molecule involved in the differentiation of pstO (prestalk-O) cells
CC (PubMed:16906151). The three-step process begins with the formation of
CC (2,4,6-trihydroxyphenyl)-1-hexan-1-one (THPH) by the polyketide
CC synthase StlB (PubMed:16906151). THPH is then dichlorinated by the
CC flavin-dependent halogenase ChlA (PubMed:20231486). The last step of
CC DIF-1 biosynthesis is the O-methylation of dichloro-THPH (or des-
CC methyl-DIF-1) by the methyltransferase DmtA to yield DIF-1
CC (PubMed:9446571). {ECO:0000269|PubMed:16906151,
CC ECO:0000269|PubMed:20231486, ECO:0000269|PubMed:9446571}.
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 Evidence={ECO:0000269|PubMed:16906151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11129;
CC Evidence={ECO:0000269|PubMed:16906151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + hexanoyl-CoA + 3 malonyl-CoA = 2,4,6-
CC trihydroxyphenylhexan-1-one + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:64352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:62620, ChEBI:CHEBI:150865;
CC Evidence={ECO:0000269|PubMed:16906151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64353;
CC Evidence={ECO:0000269|PubMed:16906151};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:A0A0K0MCJ4};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- DEVELOPMENTAL STAGE: Expressed during development. Coordinately
CC expressed with dmtA. {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 -!- DISRUPTION PHENOTYPE: Developed to the slug stage, in which dif-1
CC accumulation is maximal, though the Steely2- mutant slugs were thin and
CC tended to break up. However, two independent Steely2 mutant strains
CC both failed to accumulate any detectable dif-1 at this or any other
CC stage of development. {ECO:0000269|PubMed:16906151}.
CC -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC synthase genes localized in chromosome 5.
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}.
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DR EMBL; AAFI02000171; EAL62021.1; -; Genomic_DNA.
DR RefSeq; XP_635518.1; XM_630426.1.
DR SMR; Q54FI3; -.
DR STRING; 44689.DDB0234163; -.
DR PaxDb; Q54FI3; -.
DR EnsemblProtists; EAL62021; EAL62021; DDB_G0290853.
DR GeneID; 8627855; -.
DR KEGG; ddi:DDB_G0290853; -.
DR dictyBase; DDB_G0290853; stlB.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q54FI3; -.
DR OMA; KDVQHYT; -.
DR PhylomeDB; Q54FI3; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q54FI3; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0106265; F:THPH synthase activity; IEA:RHEA.
DR GO; GO:0048102; P:autophagic cell death; IMP:dictyBase.
DR GO; GO:0031148; P:DIF-1 biosynthetic process; IMP:dictyBase.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:dictyBase.
DR GO; GO:0030639; P:polyketide biosynthetic process; IDA:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP: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 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_N.
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; 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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 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 SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 3.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2968
FT /note="Polyketide synthase 37"
FT /id="PRO_0000377902"
FT DOMAIN 2421..2498
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 33..406
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT REGION 624..950
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT REGION 1031..1345
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT REGION 1522..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1718..2053
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT REGION 2083..2277
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT REGION 2379..2400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2568..2589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2707..2968
FT /note="Chalcone synthase"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16906151"
FT COMPBIAS 2568..2585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 718
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2458
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2968 AA; 329909 MW; 98AA21F6256A8A57 CRC64;
MNNNKSINDL SGNSNNNIAN SNINNYNNLI KKEPIAIIGI GCRFPGNVSN YSDFVNIIKN
GSDCLTKIPD DRWNADIISR KQWKLNNRIG GYLKNIDQFD NQFFGISPKE AQHIDPQQRL
LLHLAIETLE DGKISLDEIK GKKVGVFIGS SSGDYLRGFD SSEINQFTTP GTNSSFLSNR
LSYFLDVNGP SMTVNTACSA SMVAIHLGLQ SLWNGESELS MVGGVNIISS PLQSLDFGKA
GLLNQETDGR CYSFDPRASG YVRSEGGGIL LLKPLSAALR DNDEIYSLLL NSANNSNGKT
PTGITSPRSL CQEKLIQQLL RESSDQFSID DIGYFECHGT GTQMGDLNEI TAIGKSIGML
KSHDDPLIIG SVKASIGHLE GASGICGVIK SIICLKEKIL PQQCKFSSYN PKIPFETLNL
KVLTKTQPWN NSKRICGVNS FGVGGSNSSL FLSSFDKSTT ITEPTTTTTI ESLPSSSSSF
DNLSVSSSIS TNNDNDKVSN IVNNRYGSSI DVITLSVTSP DKEDLKIRAN DVLESIKTLD
DNFKIRDISN LTNIRTSHFS NRVAIIGDSI DSIKLNLQSF IKGENNNNKS IILPLINNGN
NNNNNNNNSS GSSSSSSNNN NICFIFSGQG QQWNKMIFDL YENNKTFKNE MNNFSKQFEM
ISGWSIIDKL YNSGGGGNEE LINETWLAQP SIVAVQYSLI KLFSKDIGIE GSIVLGHSLG
ELMAAYYCGI INDFNDLLKL LYIRSTLQNK TNGSGRMHVC LSSKAEIEQL ISQLGFNGRI
VICGNNTMKS CTISGDNESM NQFTKLISSQ QYGSVVHKEV RTNSAFHSHQ MDIIKDEFFK
LFNQYFPTNQ ISTNQIYDGK SFYSTCYGKY LTPIECKQLL SSPNYWWKNI RESVLFKESI
EQILQNHQQS LTFIEITCHP ILNYFLSQLL KSSSKSNTLL LSTLSKNSNS IDQLLILCSK
LYVNNLSSIK WNWFYDKQQQ QQSESLVSSN FKLPGRRWKL EKYWIENCQR QMDRIKPPMF
ISLDRKLFSV TPSFEVRLNQ DRFQYLNDHQ IQDIPLVPFS FYIELVYASI FNSISTTTTN
TTASTMFEIE NFTIDSSIII DQKKSTLIGI NFNSDLTKFE IGSINSIGSG SSSNNNFIEN
KWKIHSNGII KYGTNYLKSN SKSNSFNEST TTTTTTTTTT KCFKSFNSNE FYNEIIKYNY
NYKSTFQCVK EFKQFDKQGT FYYSEIQFKK NDKQVIDQLL SKQLPSDFRC IHPCLLDAVL
QSAIIPATNK TNCSWIPIKI GKLSVNIPSN SYFNFKDQLL YCLIKPSTST STSPSTYFSS
DIQVFDKKNN NLICELTNLE FKGINSSSSS SSSSSTINSN VEANYESKIE ETNHDEDEDE
ELPLVSEYVW CKEELINQSI KFTDNYQTVI FCSTNLNGND LLDSIITSAL ENGHDENKIF
IVSPPPVESD QYNNRIIINY TNNESDFDAL FAIINSTTSI SGKSGLFSTR FIILPNFNSI
TFSSGNSTPL ITNVNGNGNG KSCGGGGGST NNTISNSSSS ISSIDNGNNE DEEMVLKSFN
DSNLSLFHLQ KSIIKNNIKG RLFLITNGGQ SISSSTPTST YNDQSYVNLS QYQLIGQIRV
FSNEYPIMEC SMIDIQDSTR IDLITDQLNS TKLSKLEIAF RDNIGYSYKL LKPSIFDNSS
LPSSSSEIET TATTKDEEKN NSINYNNNYY RVELSDNGII SDLKIKQFRQ MKCGVGQVLV
RVEMCTLNFR DILKSLGRDY DPIHLNSMGD EFSGKVIEIG EGVNNLSVGQ YVFGINMSKS
MGSFVCCNSD LVFPIPIPTP SSSSSSNENI DDQEIISKLL NQYCTIPIVF LTSWYSIVIQ
GRLKKGEKIL IHSGCGGVGL ATIQISMMIG AEIHVTVGSN EKKQYLIKEF GIDEKRIYSS
RSLQFYNDLM VNTDGQGVDM VLNSLSGEYL EKSIQCLSQY GRFIEIGKKD IYSNSSIHLE
PFKNNLSFFA VDIAQMTENR RDYLREIMID QLLPCFKNGS LKPLNQHCFN SPCDLVKAIR
FMSSGNHIGK ILINWSNLNN DKQFINHHSV VHLPIQSFSN RSTYIFTGFG GLTQTLLKYF
STESDLTNVI IVSKNGLDDN SGSGSGNNEK LKLINQLKES GLNVLVEKCD LSSIKQVYKL
FNKIFDNDAS GSDSGDFSDI KGIFHFASLI NDKRILKHNL ESFNYVYNSK ATSAWNLHQV
SLKYNLNLDH FQTIGSVITI LGNIGQSNYT CANRFVEGLT HLRIGMGLKS SCIHLASIPD
VGMASNDNVL NDLNSMGFVP FQSLNEMNLG FKKLLSSPNP IVVLGEINVD RFIEATPNFR
AKDNFIITSL FNRIDPLLLV NESQDFIINN NINNNGGGGD GSFDDLNQLE DEGQQGFGNG
DGYVDDNIDS VSMLSGTSSI FDNDFYTKSI RGMLCDILEL KDKDLNNTVS FSDYGLDSLL
SSELSNTIQK NFSILIPSLT LVDNSTINST VELIKNKLKN STTSSISSSV SKKVSFKKNT
QPLIIPTTAP ISIIKTQSYI KSEIIESLPI SSSTTIKPLV FDNLVYSSSS SNNSNSKNEL
TSPPPSAKRE SVLPIISEDN NSDNDSSMAT VIYEISPIAA PYHRYQTDVL KEITQLTPHK
EFIDNIYKKS KIRSRYCFND FSEKSMADIN KLDAGERVAL FREQTYQTVI NAGKTVIERA
GIDPMLISHV VGVTSTGIMA PSFDVVLIDK LGLSINTSRT MINFMGCGAA VNSMRAATAY
AKLKPGTFVL VVAVEASATC MKFNFDSRSD LLSQAIFTDG CVATLVTCQP KSSLVGKLEI
IDDLSYLMPD SRDALNLFIG PTGIDLDLRP ELPIAINRHI NSAITSWLKK NSLQKSDIEF
FATHPGGAKI ISAVHEGLGL SPEDLSDSYE VMKRYGNMIG VSTYYVLRRI LDKNQTLLQE
GSLGYNYGMA MAFSPGASIE AILFKLIK
