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Probable polyketide synthase 37 (dipks37) [Includes: Polyketide synthase stlB (EC 2.3.1.-); Chalcone synthase stlB (EC 2.3.1.74) (Steely2)]

 PKS37_DICDI             Reviewed;        2968 AA.
Q54FI3;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
23-MAY-2018, entry version 102.
RecName: Full=Probable polyketide synthase 37;
Short=dipks37;
Includes:
RecName: Full=Polyketide synthase stlB;
EC=2.3.1.-;
Includes:
RecName: Full=Chalcone synthase stlB;
EC=2.3.1.74;
AltName: Full=Steely2;
Name=stlB; Synonyms=pks37; ORFNames=DDB_G0290853;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=16906151; DOI=10.1038/nchembio811;
Austin M.B., Saito T., Bowman M.E., Haydock S., Kato A., Moore B.S.,
Kay R.R., Noel J.P.;
"Biosynthesis of Dictyostelium discoideum differentiation-inducing
factor by a hybrid type I fatty acid-type III polyketide synthase.";
Nat. Chem. Biol. 2:494-502(2006).
[3]
IDENTIFICATION.
PubMed=17660200; DOI=10.1093/bioinformatics/btm381;
Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J.,
Kessin R.H., Hranueli D.;
"Polyketide synthase genes and the natural products potential of
Dictyostelium discoideum.";
Bioinformatics 23:2543-2549(2007).
-!- FUNCTION: Does make the polyketide skeleton of dif-1.
{ECO:0000269|PubMed:16906151}.
-!- CATALYTIC ACTIVITY: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA +
naringenin chalcone + 3 CO(2).
-!- COFACTOR:
Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
Evidence={ECO:0000250};
Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
-!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
biosynthesis.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Expressed during development. Coordinately
expressed with dmtA. {ECO:0000269|PubMed:16906151}.
-!- DOMAIN: Modular protein possessing six classical catalytic domains
and a type III polyketide synthase domain. May facilitate covalent
transfer of steely N-terminal acyl products directly to the C-
terminal type III PKS active sites, which catalyze both iterative
polyketide extension and cyclization.
-!- DISRUPTION PHENOTYPE: Developed to the slug stage, in which dif-1
accumulation is maximal, though the Steely2- mutant slugs were
thin and tended to break up. However, two independent Steely2
mutant strains both failed to accumulate any detectable dif-1 at
this or any other stage of development.
{ECO:0000269|PubMed:16906151}.
-!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
synthase genes localized in chromosome 5.
-!- MISCELLANEOUS: In reference to their hybrid nature and to their
discovery in D.discoideum, authors term these type I FAS-type III
PKS fusion enzymes 'steely'. {ECO:0000305|PubMed:16906151}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AAFI02000171; EAL62021.1; -; Genomic_DNA.
RefSeq; XP_635518.1; XM_630426.1.
ProteinModelPortal; Q54FI3; -.
STRING; 44689.DDB0234163; -.
PaxDb; Q54FI3; -.
PRIDE; Q54FI3; -.
EnsemblProtists; EAL62021; EAL62021; DDB_G0290853.
GeneID; 8627855; -.
KEGG; ddi:DDB_G0290853; -.
dictyBase; DDB_G0290853; stlB.
eggNOG; KOG1202; Eukaryota.
eggNOG; COG3321; LUCA.
eggNOG; COG3424; LUCA.
InParanoid; Q54FI3; -.
PhylomeDB; Q54FI3; -.
Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
Reactome; R-DDI-199220; Vitamin B5 (pantothenate) metabolism.
Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
UniPathway; UPA00154; -.
PRO; PR:Q54FI3; -.
Proteomes; UP000002195; Chromosome 5.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IC:dictyBase.
GO; GO:0016210; F:naringenin-chalcone synthase activity; IEA:UniProtKB-EC.
GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0031148; P:DIF-1 biosynthetic process; IMP:dictyBase.
GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0010629; P:negative regulation of gene expression; IGI:dictyBase.
GO; GO:0030639; P:polyketide biosynthetic process; IDA:dictyBase.
GO; GO:0010628; P:positive regulation of gene expression; IGI:dictyBase.
GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.40.366.10; -; 1.
Gene3D; 3.40.47.10; -; 3.
InterPro; IPR001227; Ac_transferase_dom_sf.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR013154; ADH_N.
InterPro; IPR012328; Chalcone/stilbene_synth_C.
InterPro; IPR001099; Chalcone/stilbene_synthase_N.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020843; PKS_ER.
InterPro; IPR013968; PKS_KR.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF08240; ADH_N; 1.
Pfam; PF02797; Chal_sti_synt_C; 1.
Pfam; PF00195; Chal_sti_synt_N; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF08659; KR; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00829; PKS_ER; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF50129; SSF50129; 2.
SUPFAM; SSF51735; SSF51735; 2.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53901; SSF53901; 4.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
2: Evidence at transcript level;
Acyltransferase; Complete proteome; Membrane; Multifunctional enzyme;
Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 2968 Probable polyketide synthase 37.
/FTId=PRO_0000377902.
TRANSMEM 1839 1859 Helical. {ECO:0000255}.
TRANSMEM 1869 1889 Helical. {ECO:0000255}.
DOMAIN 2421 2498 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 179 232 Beta-ketoacyl synthase.
REGION 708 742 Acyl/malonyl transferase.
REGION 2707 2968 Chalcone synthase.
COMPBIAS 2 28 Asn-rich.
COMPBIAS 465 469 Poly-Thr.
COMPBIAS 475 479 Poly-Ser.
COMPBIAS 585 588 Poly-Asn.
COMPBIAS 597 608 Poly-Asn.
COMPBIAS 609 617 Poly-Ser.
COMPBIAS 618 621 Poly-Asn.
COMPBIAS 674 677 Poly-Gly.
COMPBIAS 978 982 Poly-Gln.
COMPBIAS 1076 1082 Poly-Thr.
COMPBIAS 1170 1180 Poly-Thr.
COMPBIAS 1346 1355 Poly-Ser.
COMPBIAS 1524 1528 Poly-Gly.
COMPBIAS 1535 1543 Poly-Ser.
COMPBIAS 1683 1686 Poly-Ser.
COMPBIAS 1821 1826 Poly-Ser.
COMPBIAS 2376 2381 Poly-Gly.
COMPBIAS 2567 2571 Poly-Ser.
ACT_SITE 198 198 For beta-ketoacyl synthase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 718 718 For acyl/malonyl transferase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 2747 2747 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 2458 2458 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
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


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