ID   PKS40_DICDI             Reviewed;        2552 AA.
AC   Q54ED7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable polyketide synthase 40;
DE            Short=dipks40;
DE            EC=2.3.1.-;
GN   Name=pks40; ORFNames=DDB_G0291614;
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 and clustered as a pair pks40/pks41 in chromosome 6.
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DR   EMBL; AAFI02000177; EAL61791.1; -; Genomic_DNA.
DR   RefSeq; XP_635303.1; XM_630211.1.
DR   AlphaFoldDB; Q54ED7; -.
DR   SMR; Q54ED7; -.
DR   PaxDb; Q54ED7; -.
DR   EnsemblProtists; EAL61791; EAL61791; DDB_G0291614.
DR   GeneID; 8628247; -.
DR   KEGG; ddi:DDB_G0291614; -.
DR   dictyBase; DDB_G0291614; pks40.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54ED7; -.
DR   PhylomeDB; Q54ED7; -.
DR   PRO; PR:Q54ED7; -.
DR   Proteomes; UP000002195; Chromosome 6.
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   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; 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; 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; 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; 2.
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..2552
FT                   /note="Probable polyketide synthase 40"
FT                   /id="PRO_0000371397"
FT   DOMAIN          2467..2546
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          160..213
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          629..662
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        179
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         2505
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2552 AA;  289094 MW;  0515D8D76EBCB4FA CRC64;
     MDYKNKYQSN ENCNKVAIIG IGFRFPNLKG DLTPNGLWSQ LLNKYDGIVK NDRWNESFYK
     TGDIPTKYAG LIPFEELKSF DPLFFGINPS EVIHMCPQQR ILLKCTWEAL EDSGIDPIEI
     RDSNTSVFLG CSNFDYQNLN KNNNKIQQNI FASSSHSVSN RISYCFDLHG ESMTIDTACS
     SSSNAIRRGY KSIIDGSSNI SVVGGINILL DPNTSKSYSQ LNMLGKDGKC KTFDADADGY
     VRSESAGIAI LKNLNDAIKD GNNIYCVIDG SASNVDGNGF SDKSNFYSPS KSSQVECIRL
     ALESTNGGVN ENDIVYFEAH GTGTPTGDPI ELESVSIALK TSENRSSNNP LLIGSFKPNI
     GHSECASGIS SLIKCCLILK NQCFVPNINY NKPNPNIKFN QWNLKVVTDP IDFSTLKLSN
     KPISIAINNF GVTGSNCCLI VSSFKGNQTN NNNNKSKSPK QYLIPFSTNS IKSLDLYKSR
     IDNNVEFKEF AENQIKSKSK KLIQRSVAIA SNWDEFNLKS NTINTSNDKL TSNMLVSSNK
     KNATMVFVFC GQGAQYSTMA KNLYDNEPIF KKSMDKIDSK LSEYYGFSIL EKLRSFNEND
     LKGIQYSIIA QPSTCMVQIS LFELYCHWGI KPSIIVGHSL GEISSSYCSG MIDLDTFCYL
     IYHRSMVQSK TNGLGRMLSI SIGENEYNSK YSSRYPELEI ACYNSPSSIV IAGKELILNE
     IIKELKQDGV FCTILGSPTS FHTSSQIPVK DEILKISFKS KQSTYPIFST VTTNLYDEMN
     PFDTKYVYDN IINPVRFTNT ISNIYKHIEL NYSVNNNSNE IIFIEIAPHP TLSFYLKQMV
     PEDKKQSVSI FSPLSKKKSN DLFEIQKLIS ELYCLGYNGI GFNIQLSNLN ENDNIQTSLS
     LPLYQWEEQE YWKLDSLYQH HLSNGPSINH LGISNSNHTP YIKSYQTHID IQKKPFQWLK
     GHQIKGKYYF PGCGYIDNIL KIFGDNSEST TNPNKELPDI LISFIEFKTP LIFMDGVNQC
     LQTNIHSTGK KEYKALFHFK DEKSSSDWVQ TSTANFQLFS RGQGLNEDDE ESLFKYNIND
     LISNQCNLTK LSKQELYSHI KTKCGLNYSG DFQRVEKCYF GNNCSLSELS LSQGVNENRS
     TFFDSSIIDC CLHGSIGLID ENCQLVFEKL EGLTYYSSKV PTTTSQHSKI YVYSKLKPRI
     GDSYSASIIV MLENGTVLFE MENASFKSTT KIKDSLAMEY PTNEIYSCYL QSKDSLIPSL
     SSFDHIFKRK ITDEYVDQIK IYESFIPKLL FSNINKRCPE ITIAEIQSSE IEQLLLKYYK
     IKEDNDNKWL SRLFTFAFES IKQWYHNEDY DFENVLSPHN FKIFSKSTKI ISKLLFPLEN
     DNDEDSPQSL FEGGLLDKFY SSGFSAQNEL VGEIIQESIK PILNEKLVFR ILEFGGGVGS
     LSLLVLEKIN SLLIQYPNYQ IDIEYTWSDI SPSFITEAKA KFEKFNDRVN IIYKALNLEQ
     PLIGEKQGLK PQYFDYIIMF NVLHVIKDVK YGVEQIYQLL VPNGHLLFIE PIYKSIVGDG
     IFGVFDQWWS FQDTEIRKDR CCMNQQTWYK LLKSVNFNDD IKMTPELTCF VIQAQKPSIS
     NLSFSKSETT NYNNIIVFGN KDDSNLSNNF IKSIDNGNLQ FISTIEEFNK MTKYISNESI
     IYFIKSIDEL SVDNFVNITH EYTQINQKLM ELNSKCKHVL ITNDSTTTNY LSSSLIGAAR
     YYHECPLELF ILNFDTPSII ENQNLFKTIE PLINSSINIQ REFIINNHKV YYERIKNETK
     LKSIFKNSSS FESLEQVDNF MISLTPNLEY KVKVKPTSIL KENEVEIKVM STGLNYKDYL
     IYAGLVESVE PIFGIEFSGI ITNIGSGNKE FKVGDSVYGT GKSTTSSHII TDIDVISHKP
     SNISHSEASS IPVVYLTSYH SLYNIGALKN NETILIHSAT GGVGLSTLEI LKWKGHSGLI
     FVTVGSNEKE EYLRENYGDM ISGIYSTRNK NFVKQIKSKI SKLNPFGKSG VDFILNTLSS
     SDYMDSNFKC LNMSGRIVDL SITHLNSNEF TDNKKFKYNY GYHNIELQYV DKKIIKSTLS
     IISNAVSSND LQLIPITEYS IENVKDSIEF INERVHMGKI VVDHENQDSI INELIEKQKS
     IDKFDQSIFK QNYKLEPSLL GKNILITGQS GIVLEILKWI LRNSENNSID NIIILSKSSI
     KWEMELLINK TKLLNSNSIN SMGNYLNKIK FHFKSVDISD SGLTDKGIHE LLIENPDINN
     IDSIFHFAYT QATCNSDEVD LHHLTQSHSA KSMGAINLHN QSIKRNWKII NFIMSSSITS
     KTSSANQCGY ISSNNVLDAL SKYRISIGLP TICTNYGLIQ STGFVSRNES VAALLSGEGL
     LPISTNLILG TLDLQLQNQA QSSNLILSNF NFTSLNGLPQ KSLISKFDYQ ININEENEKS
     KSLLKDDNVE LTVDQLITFK ISELLSTDIL KLNKDIILVD YGVDSLVIIQ LKNWVDKEFS
     IPNALTIQQV QNSTINSFIQ LVKNSIDKKN KK