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 27-MAR-2024, entry version 115.
DE RecName: Full=Probable polyketide synthase 40;
DE Short=dipks40;
DE EC=2.3.1.-;
GN Name=pks40; ORFNames=DDB_G0291614;
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 -!- 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 STRING; 44689.Q54ED7; -.
DR PaxDb; 44689-DDB0235302; -.
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 CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 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; 2.
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.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
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 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; 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; 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; 2.
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 Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2552
FT /note="Probable polyketide synthase 40"
FT /id="PRO_0000371397"
FT DOMAIN 13..443
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 928..1235
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2467..2546
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 629..662
FT /note="Acyl/malonyl transferase"
FT REGION 928..1063
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1087..1235
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 179
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 320
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 639
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 962
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1149
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
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
//
