ID   PKS9_DICDI              Reviewed;        2931 AA.
AC   Q86AE3; Q55AX7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable polyketide synthase 9/36;
DE            Short=dipks36;
DE            Short=dipks9;
DE            EC=2.3.1.-;
GN   Name=pks9; ORFNames=DDB_G0271530;
GN   and
GN   Name=pks36; ORFNames=DDB_G0295659;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12796308; DOI=10.1128/ec.2.3.627-637.2003;
RA   Maeda M., Sakamoto H., Iranfar N., Fuller D., Maruo T., Ogihara S.,
RA   Morio T., Urushihara H., Tanaka Y., Loomis W.F.;
RT   "Changing patterns of gene expression in Dictyostelium prestalk cell
RT   subtypes recognized by in situ hybridization with genes from microarray
RT   analyses.";
RL   Eukaryot. Cell 2:627-637(2003).
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).
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}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Enriched 2.5 fold in prestalk cells.
CC       {ECO:0000269|PubMed:12796308}.
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 and clustered as a quintuplet pks5/pks6/pks7/pks8/pks9
CC       in chromosome 2.
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DR   EMBL; AAFI02000006; EAL71629.1; -; Genomic_DNA.
DR   EMBL; AAFI02000169; EDR41033.1; -; Genomic_DNA.
DR   RefSeq; XP_001733037.1; XM_001732985.1.
DR   RefSeq; XP_645569.1; XM_640477.1.
DR   SMR; Q86AE3; -.
DR   STRING; 44689.DDB0231390; -.
DR   PaxDb; Q86AE3; -.
DR   EnsemblProtists; EAL71629; EAL71629; DDB_G0271530.
DR   EnsemblProtists; EDR41033; EDR41033; DDB_G0295659.
DR   GeneID; 8618022; -.
DR   GeneID; 8627807; -.
DR   KEGG; ddi:DDB_G0271530; -.
DR   KEGG; ddi:DDB_G0295659; -.
DR   dictyBase; DDB_G0295659; pks36.
DR   dictyBase; DDB_G0271530; pks9.
DR   eggNOG; KOG1202; Eukaryota.
DR   eggNOG; KOG1221; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q86AE3; -.
DR   PhylomeDB; Q86AE3; -.
DR   PRO; PR:Q86AE3; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   Proteomes; UP000002195; Chromosome 5.
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; IPR013154; ADH_N.
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; 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; IPR010080; Thioester_reductase-like_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_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; PF07993; NAD_binding_4; 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   2: Evidence at transcript level;
KW   Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2931
FT                   /note="Probable polyketide synthase 9/36"
FT                   /id="PRO_0000376884"
FT   TRANSMEM        2293..2313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2553..2573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2429..2506
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          162..215
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          635..668
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        181
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        645
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2466
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2931 AA;  333274 MW;  5E07E9593E07C788 CRC64;
     MGNLKNINLK EKGVAIVGIG FRIPSGNNEN SISSPDDLFN NLKNGFDGVS STSERWSDNF
     HKLGEISSPN AGLLPFKEWK SFDPLFFGIN PSEAPLIDPQ QRLLLKCTWE ALEDASIDPI
     SIRGTNTSVF IGSSTIDYLH TNKHQDSVLK NAIAQSTSAI SNRISYCFDF NGPSLSIDTA
     CSSSLNAVSQ GYHSILNGTS NMSIVGGVNL ILDVDIIKAY SILSMLSKTH GKCKTFDESG
     DGFTRGECVG VVVLKNLQDA VKDGNRIYCV INGSSSNVDG NGNMDKVNFY SPSKQSQFNN
     INSAFKSTND KLSINDIQYI EAHGTGTKTG DPIETEAISM AFKNRDKSTP ILIGSIKSNI
     GHCEAGSGVA SLIKCCLMFK YQCFLPNIHF KNPNPLIKFN EWNLKVVTSP IPFNKRNNEK
     PVSMMINNFG VTGSNCCLLI SEFKNNNNFK ENINLESQSV NDRVLIPFSA NSSNSLNQYQ
     SKFKNIINNQ FNFIDFTANQ IYSKSNFLYQ RSVVIASNSN ELFENISNKK QIQTKNSIIS
     NMSFKGKNPI TIFVFSGQGS QYPKMALELY NNEVIFKKSI DLIDSKLSKY YGFSVWEKVK
     TIKDDDLTSI HDPIFAQPAL CMISVSLFEL YYHWGVNPSF ILGHSLGEIS ASYCSGMIDL
     DTFCYTVYQR SIAQSKTNGC GRMLSINISD EEFKSMYSQK YPQIEIACYN SPQSIVVAGN
     ESILNEISKE LKEKEIFTTM LGSLSSFHTS SQQCTKDSIL QLNIESNQPK VPIFSTVTTN
     LFNESNRFNS QYVYDNIIKP VKFTQTISNI YKHIESNQLN NEIVFIEIAP HPTLLFYIKQ
     MVPSSLNESV SVYSALHKKK NDVEEFQQTI SNLYCQNGYN INFKCQFNNK KSNQSINLPL
     YQWDEELYFT QAQTLEQHRK EGPPIDHLGT SNSYNSPFNN SYRTSIDIKN KPFLYLKGHM
     VKGKYYFPGC GYIDNIIQLY KNQDIFISFI EFKTPLILIE GINQYLQTNI QQTGKSEYRA
     QFHFKDQKSN EWIQSSNANF QLLDHGNDIP PKYNIKEIIE NKCNLSKLTK NELYTHIKSK
     TGLNYTGVFQ GVTECYIGGD CTLSVVSLES QTNSFLNIPI LDTCLHGMIG LSNDQCQIVF
     DKAIGFKYYS SNIPANLKDY KDSVYVYSHL KSKSVDSFFG SIIVMLSDGS VLYEIEEVVC
     KSLIPIKDSL KIEYPNDELY KVHLQSKDSP IPTPSSFKSI IYENDFFHSA LNIPEDLFKY
     ISTLFYKDII KRCPEININK INSHSVNEII SSFSKISKHE RLFRFVFETI KENGILNSLE
     ENDDAYFEFN EVIIKSSRII SKLLFPLESD NDNEDLPQSL FQNGLMDKIY KCRYLRKKNQ
     MISHVIKHSI KEIINNNIII RILEFGGGTA SLSVEVIEEI IALLQENPNY QVEIEYTWSD
     ISPAFIADAK NKINKIINDA AITNGFNVIY RPLKIDESLI ETQSINPSYY DFVIMSNVLH
     VVKNIKQAVE QMYQLLTPNG QLLFLEPPYK SVLNDSIVGS FEQWWSFTDT DIRKDRCSMS
     QQSWCQLLKT CNFKDIAMSK ECIFVGIVIH AQKPPISLLN SQPKRDNIII YGGGNPIFVE
     NIKLYSNSKS LIQIETIQEF NQLLSQSTIT NDSIIYFIKT LETLSLDNFK QITLEYIEIN
     RKLLQINSLC KHVLIVSDSR KTNYLASSVV GAARYFDEFQ QLKLNTLDFD YDSTQNYINS
     NNKDMVQFIN ILTDSKTNVH KEMIIINNKV YYEIVQKEKN LKLKYNSESF ENQNNLMCSL
     SPNLEYQLQS KQIKLRDNQV EVKTIATGIN YKDYLNFSGS NSNGDDNTGL PQFGYEFSGI
     ITRVGNNVKD YKVGDNVFGL SNSCTSSHIV TNYKKIQIKP SNLSHNEASS IPIDYLTSFM
     SLFNIGSLNI EDNESILIHL GSDGFGLSTF EILKWKGFNS NLFVTVNSYE TKRYLQDNYG
     DFITGIYSNT DKSYVTEINK KLIKLGSKKK GVDLILNTLP SDFMDSNFKL LAKYGRIIDL
     TSNHLNQSEF LKNINFKYNH GYHNFELSLI QKNKIHKCLY EISNAFENGE LKTIPIKEFT
     NLNIKDAIKY ITNNKIEKIT VSHDHEIYSD IIYRSLDEKE FSILKSNYQI NSNNLGKNIL
     VTGQSGIILE ILKWIIKYSN INTIENVIIL SRSSLKWELE LLINETKLSN NNIKFHFKSV
     DIGDSEQVDN AINEILNENQ QITNIDSIYH FAFQQITCKV QEINMKHLDI SHGAKSMGAI
     NLHNQSIKRN WKLINFVMAS SAISLIGSTD LCTYVCANAL LDSFSKYRES LGLPSTCICL
     GAIESTGFVS KNESVSVFLD GGGFHPTPIN QVLGLLDLQI QNAGKFTNSM LSNFKPSKFK
     NNQQTSLFLK FDYLMNLKNN SEETKIENTG NKNIDELFIE KVSELFSMDE SKINKNLRLI
     DYGADSLIIV QLKNWIDKEI GINLITIQQL QNNTISTSMK MILNSLMKNN QNIDDNNKDL
     PSNRIDYWKN EMKFEESIKP ISNEIQSRNN SEKIILLTGT TGFLGGFLLF NMVRLDSCKL
     IYCLIRNKSK SNNPLDEIIN NLKYHQLYEK LNQSQISKII PIIGDLSMNK LGLSNDDYET
     ISKNVNLIIN PGADINQKSS YQDCKLVNVN GVKEIIKLSL SSLKQRIPIV NFSSFSVFFN
     QSLDKNFDES VLPSIDNIDN LPTEYMKSKV VGEYILLEAS KKYNIPSILI RPPSIFLNPE
     TGIGHISDFS LLSIQSCYEL GYYPNQFEND FILINTITWL SNNITNIIMN DNCWTDSKMN
     IYNVHGKQIQ SSLIIKPLEK HFNCKHINTN DWIDMVNNSN KKSCIKLKSF HSLDIILKSE
     NNRYKPNENQ SISLSTKSLL ESMGSYNTDL EITDKMIISH INQIFNLNET I