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 27-NOV-2024, entry version 131.
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 (Social amoeba).
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.Q86AE3; -.
DR PaxDb; 44689-DDB0231390; -.
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 VEuPathDB; AmoebaDB:DDB_G0295659; -.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd08954; KR_1_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR049900; PKS_mFAS_DH.
DR InterPro; IPR050444; Polyketide_Synthase.
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 PANTHER; PTHR45681:SF4; POLYKETIDE SYNTHASE 14-RELATED; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 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 11..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 925..1209
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2429..2506
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 635..668
FT /note="Acyl/malonyl transferase"
FT REGION 925..1047
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1064..1209
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 181
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 323
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 362
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 645
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 959
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1122
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
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
//
