ID   PKS19_DICDI             Reviewed;        2778 AA.
AC   Q54T36;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   23-FEB-2022, entry version 109.
DE   RecName: Full=Probable polyketide synthase 19;
DE            Short=dipks19;
DE            EC=2.3.1.-;
GN   Name=pks19; ORFNames=DDB_G0282027;
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; EAL66435.1; -; Genomic_DNA.
DR   RefSeq; XP_640415.1; XM_635323.1.
DR   SMR; Q54T36; -.
DR   STRING; 44689.DDB0235205; -.
DR   PaxDb; Q54T36; -.
DR   PRIDE; Q54T36; -.
DR   EnsemblProtists; EAL66435; EAL66435; DDB_G0282027.
DR   GeneID; 8623370; -.
DR   KEGG; ddi:DDB_G0282027; -.
DR   dictyBase; DDB_G0282027; pks19.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54T36; -.
DR   PhylomeDB; Q54T36; -.
DR   PRO; PR:Q54T36; -.
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; 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; 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..2778
FT                   /note="Probable polyketide synthase 19"
FT                   /id="PRO_0000367829"
FT   DOMAIN          2281..2358
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          157..210
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          629..662
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        639
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2318
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2778 AA;  314398 MW;  1E3CA2D73A46CBA9 CRC64;
     MEFGNKEIAI VGIGFRIPQG KESINNGSVS HLWNNLKNGF SGIVETSERW SDNINLLGEV
     NNKFGGLLPL KEWSDFDPVH FAINPSEVPL MDPQTRLLLK CTWEALEDAF IDPIDIRGSN
     TSCFIGCSTL DYSTTNRDFN ETSENYFASN VLHTISNRLS FSYDIRGPSM TIDTACSSSL
     NSITMGFQSI QNGTSNLSIV GGASLLLDPY VSKSFSFLNM LSKKGKCKPF DSEADGYIRA
     ESCGIVILKP LSDAIRDGNN IYCVINSFSS NVDGGGLNDK SNFYSPSKQS QSDNIKLALK
     SANMKASDIS FVECHGTGTP TGDPIEVEGV SMALNSSTTS TPSKPLLIGS LKSNIGHCEA
     ASGVASLIKC CLMFKNKHYA PNVNFDQPNP KINFKDWNIK VVTEAIPFTN INEKPVSMVI
     NNFGVTGSNC CLILSQFIEH SISLNGNNPS YPIESQQQIF LIPFSANSVK SLKNYEDLII
     NDNNLSTNSF KEFVKNQIYS KSKKLYQRSV LISSNWDQLK TKNKYFKTSN DKSSNITIKR
     NQPLIVIVFG GQGSQWNKMA QQLYECEPIF RSSMDKFNKE LSKYYGYSVL DKLRSIKDDD
     IISIHQPIIA QPSILMLQIS LFELYKHWGI NVSFIVGHSL GEIATSYCSG MVDFQTVCKL
     IYHRSISQNN TNGCGKMLSV NISHSEFIEL YSNKYPTIEV ACYNSPTSIV IAGNENILKE
     ISLDLKENNI FCAFLGSLSS FHTSSQNSTK NEILPLEIPS RQSTIPTFST VTTNLFNHET
     TPFNSSYVYE NIIQPVRFSQ TISNLYQHIE NNKLGNELIF IEVSPHPSLS FYLKQMIPKS
     SSYFNSVSVL TSTNKKNSND LDEIHSTISQ IYCLGYDINF KCQFNHNDDD VNSIRNNSTI
     ILPNYQFDEQ YYWKVDINFE QYRLNGPNVF NNLGKSMINY SSNNKSYESI IDINRNPFKY
     LKDHIVKGKY YFPGIGYADN IMKLYPNKDI VINNLEFLAP FVLKENVKHI LQTNVYQLGN
     TDYRVTFNIK DNKANQWVQT CTGNFQLISL KDNNNNNNNN HSSKYNINQL LSECNFTTLS
     KQEVYKYSKL RSGITHLGTF QGIEEFHFGN DLTIARIQIN YENFDINGKP VYQTFDKSFF
     NIALLDNCIQ AITGFITNSS QFVFERLEGL KVYSENIPTD KLKYKNIYCQ AKFISLEADS
     YKSSVLVLLE DGTKLLEIEH ISFRSTLPLI DELLLNNPTN ELFTNNLQCK DSLVNILSID
     NNETSSSSGS SNTVTEIIKQ TIKPIINEKI VFRILQSFSD SELSKQIIEA LNQIFDNSLQ
     EIDIEFTIID NSNDKLPTLH DSSLIFKNDI TQLKPSYYDI IINNNNDETI IKPIFNILSS
     NGLLLLIIED DIGIRFNINN LIGVGFNENK IQKSNKVIQS QKSTILSNEL TVVPNNKNDN
     IIIYCEKHSK YTNEFKKLIS NNHTNRKQTT ISNINEFNQL LPSITNDSII YFIKSMEQLE
     MNNFKQITME YIEINQQLLK HSLTCKHVLI TIDSQIKNYL SSSIIGASRY FNEFPSLNLY
     SIDFDNQLSI SSLLNKIINQ LIENSNNHIQ REYIIRNNSI YYEILKNEKN IKSNFNSNSF
     EDNDFMTLLD STNLEYKLAS KPKKLKKNEI EVKVLATGIN YKDYLIYRGL VVIDENVSIS
     KNPLGLEFSG IITRISDENK NCEFKVGDNV FGVSHDATAS HVITDVLYVS HKPNNISHIE
     AASLPIIFST CLHGMFNIGN FNIDDDEVIL IHSATGGIGL ATLEILKWKG HKSPIFVTVG
     SKDKEQYLID NYGSFITGIY SSRNKNYVNE IKSKLNQLYG TTGKFNGVDL IINTLPNEFT
     HSNFLCLKER GKIIDLSITH LNNNEFLNFN NFKFNKSYHN IEFMHINKRV VSRLLKSISN
     ALNENKVKLI PITTFQIENV KEAIEYINQR KHIGKIVLDH SCSNGSIGSD GLLNQLIESD
     NNEKNHTILK YDFKIDTKNI IGKNIIITGQ SGIILEILKW LIKYSPPTES FENIIILSKS
     SLKWELELLI NKTISRKDNN TKFHFKIVDV GDSIEMRKSI NQILLENPNI DNIDSIFHYA
     FTQVTKEVEE IDIESLDISH NAKTMGAINL HEISIEKSWK LKQFVMASSI ASLFGSFNQC
     TYVSANLVLD SLSRYRKSIG LPSTCTNWGT IKSSGFVSRN DSVSKMLDDQ GFIPIPTNII
     LGSLDLQLQN SNKYSNLIVS KFNYDSIKKF ASETSTFQRL DFILNSIKEK DNDNNGGENI
     SISESIQMKF LNKISELLSI EQSKINTDIR LGEYGADSLT SVQLKNFIDK ENKSNVITLQ
     QLQNNTIGVN IQIILEQIKK LDSNETKGKS KKIIKKDSAP SLEYWRNEMK LDESIQAIKM
     NPIDFRNDSK VFLTGATGFL GVHLLSNLIK SPNCSVVYCL IRNKKSEPNP INAIINNLKH
     HKLYHFHNEF ELSKVKVIVG NLASPLLGLS KLDFGFVSNQ INLIINSGAD INLASNYEES
     KVVNIGGLIE LIKLSTTGDY QKPIVGFSSI SVFFESPNCK EFDEETVIPT IENINNLPGG
     YMKSKVVVEN LFREAAKRGI PSMLIRLPII FSHEETGIGH DSDFFQLIIQ SCYAVKKYPN
     IDKNILTSPI GWIGLNTIKM IGNEKCWNKS SSNQLNIYSL NSEVSSIKSS FSFLEKQYGC
     EMVEYEQWKN IINQSKILSC IKFKTFHSLD RLNGVYNLGH GFGVSKKTKE LLQSMNSYEG
     GMVNEKIIQN HINYIFKN