ID   PKS21_DICDI             Reviewed;        2779 AA.
AC   B0G138;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable polyketide synthase 21;
DE            Short=dipks21;
DE            EC=2.3.1.-;
GN   Name=pks21; ORFNames=DDB_G0282029;
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 triplet pks19/pks20/pks21 in
CC       chromosome 3.
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DR   EMBL; AAFI02000044; EDR41070.1; -; Genomic_DNA.
DR   RefSeq; XP_001733001.1; XM_001732949.1.
DR   SMR; B0G138; -.
DR   STRING; 44689.DDB0235174; -.
DR   PaxDb; B0G138; -.
DR   PRIDE; B0G138; -.
DR   EnsemblProtists; EDR41070; EDR41070; DDB_G0282029.
DR   GeneID; 8623374; -.
DR   KEGG; ddi:DDB_G0282029; -.
DR   dictyBase; DDB_G0282029; pks21.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; B0G138; -.
DR   PhylomeDB; B0G138; -.
DR   PRO; PR:B0G138; -.
DR   Proteomes; UP000002195; Chromosome 3.
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; cd05235; SDR_e1; 1.
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   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; 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; IPR010080; Thioester_reductase-like_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 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; 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; 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..2779
FT                   /note="Probable polyketide synthase 21"
FT                   /id="PRO_0000371384"
FT   DOMAIN          2282..2359
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          157..210
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          632..665
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        176
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        642
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2319
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2779 AA;  314195 MW;  8853A4F20089A375 CRC64;
     MKLENKEIAI VGIGFRIPQG KESINNGSVS HLWNNLKNGF SGIVETSERW SDNINLLGEV
     NNKFGGLLPL KEWSDFDPVH FAINPSEVPL MDPQTRLLLK CTWEALEDAF IDPIDIRGSN
     TSCFIGCSTL DYSTTNRDFN ETSENYFASN VLHTISNRLS FSYDIRGPSM TIDTACSSSL
     NSIAMGFQSI QNGTSNLSIV GGVSLLLDPY ISKSFSFLNM LSKKGKCKPF DSEADGYIRA
     ESCGIVILKP LSDAIRDGNN IYCVINSFSS NVDGGGLNDK SNFYSPSKQS QSDNIKLALK
     SANMKASDIS FVECHGTGTP TGDPIEVEGV SMALNSSKTS TPSKPLLIGS LKSNIGHSEA
     ASGVASLIKC CLMFKNKHYA PNVNFDQPNP KINFKDWNIK VVTEAIPFTN NNEKPVSMVI
     NNFGVTGSNC CLILSQFIEQ SINQNGNGHS YPAESQQQQQ QRFLIPFSAN SVKSLKNYED
     LIINDIKIST NSFKEFVKNQ IYSKSKKLYQ RSVLISSNWD QLKTKNKYFK TNNDKSSNIT
     IKRNQPLVVI VFGGQGSQWN KMAQQLYECE PIFRSSMDKF NKELSKYYGY SVLDKLRSIK
     DDDIISIHQP IIAQPSILML QISLFELYKH WGINVSFIVG HSLGEIATSY CSGMVDFQTV
     CKLIYHRSIS QNNTNGCGKM LSVNISHSEF IELYSNKYPT IEVACYNSPT SIVIAGNENI
     LKEISLNLKE NNIFCAFLGS LSSFHTSSQH STKNEILPLD IPSKQSRIPT FSTVTTNLFN
     HETTPFNSSY VYENIIQPVR FSQTISNLYQ HIENNKLGNE LIFIEVSPHP SLSFYLKQMI
     PKSSSYFNSV SVLTSTNKKN SNDLDEIHST ISQIYCLGYD VNFKCQFNHN DDDVSSIRNS
     KVNISLPNYQ FDEQHYWKVD INFEQYRLNG PNVFNSLGKS MINYSSNNKS YESIIDINRN
     PFKYLKDHIV KGKYYFPGIG YADNIMKLYP NQDIIINNLE FLAPFVLKEN VKHTLQTNVY
     QLGNTDYRVT FNIKDNKTNQ WVQTCTGNFQ LISLKDNNND HSSKYDINQL LSECNFTTLS
     KQEVYKHSRS ITGITHLGAF QGIEELYFGN DCIISKIQVN TENFDIDGKP VYQTYDKSFF
     NTALLDSCSQ TIVGFITNSS QFVFERLEGL KVYSENIPTD KLKYKNIYCQ AKFISLESDS
     YKSSVLVLLE DGTKLLEMDC ISLHSTLPLL NSLLINNPTT ELFTNNLQCK DSLVNILSID
     NNQTFSSISS SNTVTEIIKQ TIKPIINEKI VFRILQSFSD LELSKQIIET LNQIFDDNSL
     QEIDIEFTII DNSNDKLPTL HDSSLIFKND ITQLKPSYYD IIINNNNDGD DETIIKSIFN
     ILSSNGLLLI IGDDIGDKYN IDSLINLGFN ENKIQKSNKV IQSQKSTILS NELTVVPNNK
     NDNIIIYCEK ESKYTNEFMK LISNNHISCK QTIISNINEF NQLLPSITND SIIYFIKSME
     QLEMNNFKQI TMEYIEINQQ LLKHSLTCKH VLITIDSQIK NYLSSSIIGT ARYFNEFPSL
     NLYSIDFDNQ LSISSLLNKI INQLIENSNN HIQREYIIRN NSIYYEILKN EKNIKSNFNS
     NSFEDNDFMT LLDSTNLEYK LASKPKKLKK NQIEVKVLAT GINYKDYLIY RGLVVIDENV
     SISKNPLGLE FSGIITRISN ENQNCEFKVG DNVFGIACDT TASHVIADVL YVSHKPENIS
     HVEAASLPVI FSTCLHGMFN IGNFNIDDDE VILIHSATGG IGLATLEILK WKGHKSPIFV
     TVGSKDKEQY LIDNYGSFIT GIYSSRNKNY VNEIKSKLNQ LYGTTGKFNG VDLIINTLPN
     EFTHSNFLCL KERGKIIDLS ITHLNNNEFL NFNNFKFNKS YHNIELMHIN KKVVSRLLKS
     ISNALNENKL KPIPITTFQI EDVKEAIEYI NQRKHIGKIV LDHSCSNGSI GSDGLLNQLI
     ESDNNEKNHT ILKYDFKIDT KNIIGKNIII TGQSGIILEI LKWLIKYSPT ESFENIIILS
     KSSLKWELEL LINKTISRKD NNTKFHFKSV DVGDPIEMRK SINQILLENP NIDNIDSIFH
     YAFAQITKEV EEIDIESLDI SHNAKTMGAI NLHEISIEKS WKLKQFVMAS SIASLFGSFN
     QCSYVSANLV LDSLSRYRKS IGLPSTCTNW GAIKSAGFVS RNELVSKMLD DQGFIPIPTN
     IILGSLDLQL QNSNKNSNLI VSKFNYDSIK KLSSETSTFQ RLDFILNSIK EKDNDSNGGE
     NSVSESIQTK ILNKISELLS IEQSKINTDI RLSDYGADSL TSVQLKNFID KDIKSNVITL
     QQLQNNTIDM NIQTILEQIK KLDSNETKGK SKNIIKKDSA PTLDYWRNEM KLDESIQAIK
     MNPIDFRNDS KVFLTGATGF LGVHLLSNLI KSPNCSVVYC LIRNKKSEPN PINAIINNLK
     HHKLYHFHNE FELSKIKVIV GNLASPLLGL SKLDFDYISN QINLIINSGA DINLASNYEE
     SKVVNIGGFI ELIKLSTTGD YQKPIVGFSS VSVFFNASNC KEFDEETVIP TIENINNLPG
     GYMKSKVVVE NLLREVAKRG IPSMLIRPPI IFSHEETGIG HDSDFFQLII QSCYAVKKYP
     KIDKNILTSP IGWISLNTIK MIGNEKCWNK SSSNQLNIYS LNSEVSAMNP SFSFLEKQYG
     CEMVEYEQWK NIINQSKILS CVKLKTFHSL DDLYNIYNLG NGFGVSKKTK ELLQSMNSYE
     GGMVNEKMIQ NHINYIFKN