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 27-NOV-2024, entry version 121.
DE RecName: Full=Probable polyketide synthase 3;
DE Short=dipks3;
DE EC=2.3.1.-;
GN Name=pks3; ORFNames=DDB_G0271000;
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=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.Q55CN6; -.
DR PaxDb; 44689-DDB0235216; -.
DR EnsemblProtists; EAL72850; EAL72850; DDB_G0271000.
DR GeneID; 8617404; -.
DR KEGG; ddi:DDB_G0271000; -.
DR dictyBase; DDB_G0271000; pks3.
DR VEuPathDB; AmoebaDB:DDB_G0271000; -.
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: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; cd05195; enoyl_red; 1.
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; 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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
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; PF13602; ADH_zinc_N_2; 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; 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 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 39..464
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 962..1255
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2330..2407
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 664..697
FT /note="Acyl/malonyl transferase"
FT REGION 962..1084
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1106..1255
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 209
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 348
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 388
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 674
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 995
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1169
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
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
//
