ID   PKS3_DICDI              Reviewed;        2837 AA.
AC   Q55CN6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable polyketide synthase 3;
DE            Short=dipks3;
DE            EC=2.3.1.-;
GN   Name=pks3; ORFNames=DDB_G0271000;
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).
CC   -!- FUNCTION: Probable polyketide synthase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: Modular protein that is responsible for the completion of one
CC       condensation-processing cycle. The beta-ketoacyl synthase region is
CC       responsible for the actual condensation reaction while the acyl/malonyl
CC       transferase region is responsible for incorporating carboxylic acids
CC       units onto an acyl carrier protein (ACP) domain (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC       synthase genes localized in chromosome 1.
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DR   EMBL; AAFI02000005; EAL72850.1; -; Genomic_DNA.
DR   RefSeq; XP_646445.1; XM_641353.1.
DR   SMR; Q55CN6; -.
DR   STRING; 44689.DDB0235216; -.
DR   PaxDb; Q55CN6; -.
DR   EnsemblProtists; EAL72850; EAL72850; DDB_G0271000.
DR   GeneID; 8617404; -.
DR   KEGG; ddi:DDB_G0271000; -.
DR   dictyBase; DDB_G0271000; pks3.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q55CN6; -.
DR   PhylomeDB; Q55CN6; -.
DR   PRO; PR:Q55CN6; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05235; SDR_e1; 1.
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; -; 1.
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; IPR013120; Far_NAD-bd.
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; 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; IPR010080; Thioester_reductase-like_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 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; PF07993; NAD_binding_4; 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; 3.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2837
FT                   /note="Probable polyketide synthase 3"
FT                   /id="PRO_0000376879"
FT   TRANSMEM        2464..2484
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2330..2407
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          190..243
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          664..697
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        209
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        674
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2367
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2837 AA;  320930 MW;  ED5EDF4FC8702549 CRC64;
     MNVSAYLPTC LPTYLPTCLP TYLPTYLPTY LPICLSEENN GIGIIGIGFR LPGGGSGKSL
     GNPSELWKEL VNGYDGIIET NERWSDNFNK LGEINNRYGG LLPMDEVKSF DPLFFGISPP
     EATAIDPQQR LLLKCTWEAI EDAMIDPINL RGSNTSVFIG NTTHEYRDLN RTIDSIQTNI
     FSSSSHSSSN RVSNIFDFHG PSITIDTACS SSSNAVVLGC KSIIEGNSKM SIVGGTSLIF
     DANTPKSFSY MNMLSKDGRC KSFDANADGY VKSECIGVLL LKDLNQAIID GDRVYCVIKG
     TSSNVDGNGY SDKSNFYSPS AQSQAENIKM ALSSGNINAK DVDYVEAHGT GTPVGDPIEV
     EGISSIFKDN HSKENPLLIG SFKSMIGHCE ASSGIASLVK CCLMFKNRYF IPNLHFKTPN
     PLIKFNEWNL KVVVEPTPFP KKEITMAVNN FGVTGSNVCI ILKDFNYNHN SSSDNNNTIN
     LKQQQHQNNI EYLIPFSANS TKSLEQYQSL ISNFNQETME FNDFVKEQIM SKSNSLYQRS
     VILGSNWNDF KDNLISTNNN IKTIKTTSSN ISIKSKNPII IMVFCGQGSQ YNTMALELYK
     NEPIFRKTMD MLDNKLSKYY GFSILEKLRS IPVDDMKSIH NPALAQPAIC MVQISLFELY
     KHWGIKPTFI VGHSLGEVTA AYCSGMIDLE TECYLIYHRS IAQSTTTGCG RMLSINISPE
     KFIEQFSSRY PDVEISCYNS PTSIVIGGKE DQLNKISEEL KSKGEFTSML GSLSSFHTSS
     QKAIKEYILS LDYKSKESEI PIFSTVTTNL FDYKTTPYSP KYTYENILKS VNFTQTIENL
     YKHIENNQLG TDIVFIELAP HPTLQFYLKQ MIPKDSSYFG KGDSISIYSP LHKKKNDVKE
     IRQTISQLYC QNGYNINFKC QFENINRSIV PTHKLPLYQW DEKQFWKINS LYENYYLTGP
     PIDILGNSIT DSPFVKSYQT FINIKRKPFQ YLKGHVVKGK FYFPGCGYID NLLKIYPSQD
     ITISTLEFST PFIFTDDSVN HCLQTNIYPT GKTEYKVLFH FKDQKKNEWI QSSFGNFQLF
     KHNGEKSLKI FNQKYNIKDL IEKRCNLTKL TKEDLYDHIK LKTGLTYSGM FQAVSMCYLG
     DNCSLSVVSL ELPKHLPDQK SFFNSSILDC CLHGMIGLVD EHCQLVFDRI EGFNLYSSNI
     PSARDQHTNV YVYSSLNAKM GDSYFASIVV MLEDGTVLIE IDNAACTSLT PIQDSLKIEA
     PTNELYSTYL QSKDSLILPP QTFESLYQQE KGQNDILVGT IIKQSLVPFV NEKMVFRILD
     FSSGFADYNG TTFHSSNNVL EKFNQLLKEF PLCEIDIEYT FGSVPQSLTS SIKDKLSHIN
     ERVSILYRDY SINDPLLLED NQLKPSQYDI VLINDLEKET NDIKATLYMI YNLMVPNGQL
     ILINNDGNNL IEIKELLDQC NFKDTIISND KKSIIQTRKP QLLSELSPNP NIDSYDQIII
     YSNDDSEICN KFLKSLESTD DKILSIISTI SKFNEFVEKQ SITDKSVIYF IKTMEQLTLD
     NFKSITFEYI EINRKLLKLN SMCKHVLITS DSRKDNYLAS SVIGAARYFD EFQQLQLFTL
     DFDKESIIEY THNNNEKNLV SLIELLTDKK ISIQKEYLIR NGKVYFERIK KEQNLRKKFK
     SESYQDLVEN DLVAVLSPNL EYELKPMTKD LEPFEVQVEI KSFALNYKDY LTYIGSVPPE
     MVNHKTGDIN DPEFGSDFSG VITRVSKNNC SEFKVGDQVY GTAYNTASSK SIIDSGSIYF
     KPNNLSHEQA STIPVVYSTS LHSIYNIGNL KNYESILIHS ASGGVGLSSL NILKWKGHCS
     YIFLTVGSPE KEKYLRDTYG SLITGIYSTR DKSYVQKIKD KLKELGSDKT GVDLILNTLS
     SDYMDSNFNC LSKSGRIVDL SITHLNSNEY IDNKKFKFNY GYHNVELLFI AAPILKKLLK
     SISKAIENNE LINNLPITQY SNVNIKNAFE YINQRKHIGK IVVNHDTDLV GNLIKEKINS
     TSNLDFTLLK SNYQININNL GKNIIVTGQS GIVFEIIKWI VKFAPLVENI IILSKSSMKW
     QLELLVNRNK HIKFHFKSVD VGDINSMGKA IDEVSNDIDN IDSIFHYAFH QITKNVEAIN
     MDTLDISFGA KTIGAIILHD QSIKRGWKLK NFIIASSVTS SLGSESQCSY VCANNVLESF
     SQYRKSLGLP SICTSYGLIK STGFVSRNEN VSVMFENLGF NPLSINTILG SLDLQIQNQE
     LSTNLIVSSF NFSNITKYNP QKNNFSKIDY QVSLEEKNKV NQLGHDGNQD NKNSVNQMFL
     EKVSEVLSIE ISKINIDIKL SAYGADSLSI VQLKNWVDKE LSGNIITIQQ LQTNTISSSI
     KIITNSLDKK KEGKNKSSTV VNNTNEITTT TKTFEYWKNE AKLDETIIAS SIKSDLIIDN
     KMDKVILLSG STGFLGGYLL LNLVKMKNCS KIYCLTRSGH LSDQIDLMNK IIDNLKHHKL
     FEMFEQSELE KIFPVRGDLR KSKLGLSDKM YLEISNQVNL ILSCGADINL NANYDEIKPT
     NVDSTKEFIK LSVSKGTNKP MIPIVNLSSF SIFFGQKLND EIEFDEYQVG IPSLSNLNNL
     PGGYIQSKLI CEHLLLEASS RGIPAMTIRL PSIFSNPHTG IGHSGDLLQL IIKSISVTKY
     FPIEPTSLFI SPVTWVAQNI INLIFNEGCW SKTKINTLNI ISLNGELQTT NEIFLMIKKN
     FNYKETTLIN WKKMISESND KTCIRLRTFH PLDFTPTKYH MSKEFKISKN TKSLLISFGS
     YDGWNITEQM VLNLLKQ