ID   PKS2_DICDI              Reviewed;        3010 AA.
AC   Q55DM7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable polyketide synthase 2;
DE            Short=dipks2;
DE            EC=2.3.1.-;
GN   Name=pks2; ORFNames=DDB_G0270572;
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   -!- 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; EAL72636.1; -; Genomic_DNA.
DR   RefSeq; XP_646104.1; XM_641012.1.
DR   SMR; Q55DM7; -.
DR   PaxDb; Q55DM7; -.
DR   PRIDE; Q55DM7; -.
DR   EnsemblProtists; EAL72636; EAL72636; DDB_G0270572.
DR   GeneID; 8617054; -.
DR   KEGG; ddi:DDB_G0270572; -.
DR   dictyBase; DDB_G0270572; pks2.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q55DM7; -.
DR   OMA; LDEMPWI; -.
DR   PhylomeDB; Q55DM7; -.
DR   PRO; PR:Q55DM7; -.
DR   Proteomes; UP000002195; Chromosome 1.
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:0099139; P:cheating during chimeric sorocarp development; IMP:dictyBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05235; SDR_e1; 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; 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; 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   3: Inferred from homology;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..3010
FT                   /note="Probable polyketide synthase 2"
FT                   /id="PRO_0000367828"
FT   DOMAIN          2482..2559
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          155..208
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          629..662
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        174
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        639
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2519
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3010 AA;  339871 MW;  52609B79E0F6FB00 CRC64;
     MIESTSNKSR DVAVIGIGLR LPGGSNTPLE LWNNLIKGID GIVETKERWS DTFSEMGEVS
     SKYAGLIDFD QWMSFDPLHF AINPSDAKEI DPQQKILLKT TWEAFEDAQI DPLSLRGSDT
     SVYVGASSMD YASINTDPNK QPINCFNVNL SGVSNRISYC YDLRGTSLTI DTACSSSLNA
     VHLGYESIVN GKSDYSIVGG VNFIINPQQS RAFKYAMVTS KTGKCKAFDE SADGFVRSEG
     AVVLILKSLS KSIEDGNQIY SIIKGSSSNV DGTLNKTNYF APSKVSQSNN MQKAFDSTNG
     ELTPNDISFF ELHGTGTQIG DPIEVEAVST LFKDIKTKES PLLIGSIKSN IGHLEPASGV
     ASLAKVCLML KNREFVKNIH FETPNPNIKF DEWKVKVCTQ NTPFPTIRGK PISIAINSFG
     ITGSNACLLL SEYLKTNITT TNDQLEPSTT SYLIPLSSSS KKSLELYKNE LTNNIETFSK
     SIEFKDFISY HINSKAIKLA SRSVLMVKDW DELKSSLNLN EPLIYSSKGN KSGNIMKDNN
     KNPILVFVFC GIGGQWNQMG KQLYETSKVF KQSIDEIDQI FNRLFGYSIL KKLRSISDDD
     SKGINEFITS QPSIFMLQVS LFEFYKSWGI NPSINVGHSF GEISSACCSG MLDLETACFI
     VYKRSIIQTK TIGSGGMLVI GLSEDEYKKQ YQSQYPLIEI SCFNSPSSIV ISGSELDLTT
     ITSSLKEKNI FTYLLGSPAA LHSSKQKVIK DDILTQLKDI KFKQPTIKTF STVTTNLFDN
     STTPFDSNYI FSNIRKPVSF EKTIKNIFNH IETNDLGSNV IFLELSPLPT LTNYIKEMIP
     QNSNYFYIDD ESITILTSLN KKKSIDELQE IKSTISQIYC SGYNVNFKSQ LTTTTTTTFG
     NLIIDSNKIV KGFTSYYLPR YQWDESNYFK VGRISKQISQ GPTATQLGYR NDVSPFMSYT
     SYIDIKEEPF KFLKCHQSRG RNLFPGNAYL ENVLKVFPDQ DLTFHLIEYR SPLILKEGIK
     HIISTNIYPS AKNEYRVTFH YKDSFDKWIL GCSARFSVLK HNSDLENQKI DVESLKAKCN
     WTTIKRKEFY EVLKTNTSLA LTGQFQCIEE AYYGYNCCLA KISMNETLTK LSQYDNELFL
     NACTIDGGFQ LLGLFRDNPD TFVMDRVELL RFYASNIPKS SKFRENYPFI YTYTEFISQI
     GNSVYANINT FLPDGTLLFN TPVVCYSSIS TDIKNQLSIE NPNHQLYSTV LQSLESPLSV
     TTQNAIIDEK LFLSFLPTPV ANIRKAFTTC IFSNIKKIYQ SITPAKINTS TVDSLIDSYF
     KICETDNIEK RKLGETLFNA LKLNYSIIEY SSQAKLIKLL STNQIEIMNK ITTHLLNETK
     PTTNTTETTP VSSSQKLPEQ IQLIENIITK SVLPLVNEKI VFRILEISSG IGQLSKIIVT
     RLNELLQQNP LAEIDIELTF TDREDITLIK EKLTTLLYST SSTADINSKD LSSRKTSLIF
     TQLDLNDKDL ISSKTIYPSY YDIIVLNGLD GIKDLNQSIE TIYQILNPNG YFIMIDTLFK
     ANKSDLKNYE LYQQWLSFNY FDSTKDLDSW KKLLTQDFKL INFTATSSQP WVILCQKPRF
     FETVSTENPI STTLSCYDQV IIFGTIDNIN ESKALSKLMD VNDRGTDIYC IKTLDEFETH
     VKETPLTDES VIVYVNTINQ VFISFISYSL EYIKINQHLL RTNCNAKHVL LTRSAFIETT
     NTLVSATVGA FRYFCEFSQL DLYLMDFDDS IYLKSMQFIN VTHEMTNPNK HYQREFIFRG
     DKVYYERVTQ ETNLKLKLKS TSYISEPTQL YAKLGQNLQY QLKPFENKIP EGFIEVKVLA
     SGINFKDNLV YRRLVPNEAV NHTGNSNDPE FGYECSGIVS RVGDGVTKFK VGDEVVGLGF
     NCTGSFVTLE QFRFVLKPKN LTHVEAASIP VVYLTSYYSL FVAGYLSIEK KESVLIHGGT
     GGIGLACINL LKAKGFKGYL FVTVGSKEKE NFLRVTYGNF ITGIYSSQNT DYLLEIKKKI
     QQLTGNNLIF KQFGVAKMGI DLIINTLSNE FMDANFNSLC QGGRIIDLSV THMNSQDTTD
     FRKFRYCISY SSVELLLNGF ERNKLILQEV MDMFVNENLA LLPIKEYSVK DIKEAIEFIA
     ERKHIGKIVV NHENYDLISQ TLVSNDNEFY KDFLIPKANY RISADCNLGK TVLLTGQLGL
     SLSIIKWIIA FNNLEQPVEN ILVLSLSPIK YELEHMICYC KHVNNQIKII FKQVDISDMC
     ALDDAIGEIY KENENLPLVS SIFHNAFAPS ECDALDIDED HLRISHSAKT MGMINLNSLS
     TGIWSESIKN FVLSSSITSI LGSQRQCGYI SANCIIDAVS RLRASEGLPC TSINWGVLGT
     GFVSRNESVS KLFEYQGFIP ISMDMLIGTL DLFLQNSGKL NNKIVASFNY NNVSAAFRNH
     HLSYKLNYFL NPVYSKGSTF DDNELSIRDD ILEKFSEYLS TEKSKLSLDI KLIDYGSSSI
     MLVELKNYLD KTYTPNILSI AQLQNVTINQ LIQAVIQAVS KLKKPTTNQQ SQQPIISNIK
     WEDEIALDPT IKPTQQIIDT YKNEMTQLYK NNNNKTSLGG LQVLLTGPCT FSGTHILSNL
     LLSSKTKVIH CLLPMETPEQ VMCTIIDNFK AQGLYDQLNL ANVLSKIKPI AADFTRPIFG
     LDTDDYIELS KKIDIVINAA SNTTKHYCAH ISYEDTNKEY LHGVSHLLRF ASSEKLKRVV
     QISTLGRYSD LQRNSLDEYY FPEVDFSFIS DQNQLVSGYI QSKIVAEYHL KQASNRGIPC
     LIVRTPFTFP GNNGIGREAD FTQLLLQSCY TLNCYPTESH IQLYTAPVTW YAKNITLMAV
     GSDISQDGCW DTINTSPIEN LLCFNLFGGG FDFGDLLVDI SKDLSWKEVP FETLVKKAAV
     NETECCKRLA SFVLKKKGDF LKNLGVIPGN FTVNENLKNY LTLNNSFDGW LVTKQLVYNH
     LSYVFKKKVF