ID   PKS29_DICDI             Reviewed;        3106 AA.
AC   Q54FQ3;
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 29;
DE            Short=dipks29;
DE            EC=2.3.1.-;
GN   Name=pks29; ORFNames=DDB_G0290699;
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 quartet pks29/pks30/pks31/pks32 in
CC       chromosome 5.
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DR   EMBL; AAFI02000167; EAL62084.1; -; Genomic_DNA.
DR   RefSeq; XP_635588.1; XM_630496.1.
DR   SMR; Q54FQ3; -.
DR   STRING; 44689.DDB0235262; -.
DR   PaxDb; Q54FQ3; -.
DR   EnsemblProtists; EAL62084; EAL62084; DDB_G0290699.
DR   GeneID; 8627785; -.
DR   KEGG; ddi:DDB_G0290699; -.
DR   dictyBase; DDB_G0290699; pks29.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54FQ3; -.
DR   OMA; GWHEFKV; -.
DR   PhylomeDB; Q54FQ3; -.
DR   PRO; PR:Q54FQ3; -.
DR   Proteomes; UP000002195; Chromosome 5.
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   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; 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; 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; PF08242; Methyltransf_12; 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; 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   Coiled coil; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..3106
FT                   /note="Probable polyketide synthase 29"
FT                   /id="PRO_0000371389"
FT   DOMAIN          2533..2610
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..234
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          661..694
FT                   /note="Acyl/malonyl transferase"
FT   REGION          2614..2656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2609..2656
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        200
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        671
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2570
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3106 AA;  353444 MW;  AE9335E3E68F0D2D CRC64;
     MVQNTDNTRN SKLIRDRNDY DDNDDVDSGD IAVIGIGLRF PSGNLKESIS KPNQLFNELL
     NGLDGIVTTS ERWSDNYYLN GEIVSKFAGL LPLDEWKQFD PIFFAINPSN DNVSSIDPQQ
     RLLLKCVWEA LEDSGIDPIS LRGTNTSTFI GSSTIDYSIL QRSPFETQNN IFGSTTHSVA
     NRIGYCFDFR GENLTIDTAC SSSSNAINCG YNSIKSNKSN VSIVGGVNFL LDPHLSKSFT
     QLGLLSPTGR CHTFSSDADG YVRSEGVGIV VLKKLKDAIK DSNNIYCVIK GSSSNIDGNF
     DKLNFYSPSK SSQCENIKLA IKSTNGQINE SDIDYCETHG TGTPTGDPIE LEGISRVFNN
     IASTTTNNNN KQVLVGSIKS NIGHTEACSG VASLIKCCLM FKNKLFLQNI NFKEPNPLIN
     FKEWGLKVVT EPIKFNENKP TVMLINNFGI TGSNVCLILS EFENNHNDYH KMEIDNKLSE
     EKKKYLIPLS SNSSTSLNNY KSSIIKHSNS STTTTTTSFK EFVYNQIKFK STSLIQKSVI
     IASDWNEFQD ENNQIKLNNS DNLISNITVE KKKSPITVMV LCGQGSQYNK MALSLYDNEP
     IFRESVNRFD KELFKYYGYS VLDKLRSIDD KDLISIHQPI LAQPANVMIQ VSLYELYKHW
     GVSADIIIGH SLGEVSSPYC SGMIDFQTLC YLTYHRSVAQ NRTTGTGRML SVNISSDEFI
     NKYQSTTKYK SLEIACYNSP TSIVIAGKED LLNEITKEFK SNDIFCSMLG SLSSFHTSSQ
     QMIKDEVCSL NISSKQPSIA VFSTVTTNLF NHQSSPFNAN YVFDNIIQPV YFTQTITNLY
     KHIESNDMGN EITFIEVSPH PTLQYYLNQM KSTQSSYFNN GKNITIYSPL NKKKNDYNEF
     LKTISLLYVK NNFDINFKSQ LINNNNNNYS NQLNNLPLYQ WDDKEYFKLN SLLEKIKSEG
     PSIHGLGNNT DSPNPSYQTF IDIKKSPFQW LKGHQVSDKF YYPGMGYVHN LLSIYPNQDI
     TISSLEFKSP LVLTEGNRQC LQTTIAPLSK NEFNIKSYYK DQKTNQWILT SLGNFSLTKH
     NSIISNKLIN IQSLKDKCNF TSISKQDFYE TIRIKTNLTY KGLFQGVKQC HIGNNCSLAI
     VSLNEIYNQK EYNHLINNSN MNTFLNTAIL DTCLHGSLVA VTQPVVLDKI EGFKYYSSNI
     PSLNKNNNNN DDNDDDIKEL YVFSDIKPRT NSQTYSISVK IILPNGTLLV DISNVVCALV
     SLDSNPDSTI ICEPPSNNIY TPYLQSKDSV INKPEQFKHL YRVDEFSVKE EDNQFLSNES
     LLSLFYKHIN NRCPSINLES LTTLEYNQFK QLYYNSSANE NLFKFIFENL KKYSNIVNLD
     NDHSNIKSKN EELFIRTTKI MAKQLFPLKD DDSITDTPQS LFESGYLDDF YKNSRVVQPL
     NSLLSEIIVE TLKPILNEPI VFRILEAGGG TGSLSLLILE KICKLLNNNS TTSIINIEFT
     WSDISASFFA EIKEKFSSFT NRNNLNIIYR VLDLEKPLLD QDLKASYYDF VVMSNVMHVV
     KKLKPTLNEI HNILTPNGQL LLIEPPHKSF IYDSVFGCFS QWWPSSDSDI ELRPDRCCMK
     QEKWINLLNQ CNYRDTIMSG NDNLLFLIQT RKPTINEIIS EQSISLDQLN SFNNIILFSN
     NNNNNNNNNS DNNRNSCSSI LDSITLNQEL KHKIININNF NEFQSWITNN QTKDDCNKTL
     IIFLKSIESI MNTSNFKEIT FEYIQINQLI LKLELSNNFK HLLLSLNSST DNYLSSSIVG
     AARYFVEFPQ LDLLTLNYDN VSIENNQQLS LINYLINPNN NIQKEFTINN NRVYYERYCR
     RSNNIKSKLQ SKSFENNKDN LCIQLNSNLE YQLYSKKDKL NSNEVEIEIK ATGMNYKDYL
     MYIGMIGTNL DIKYGKEIEN CIGFNNPKIG KDFSGIITRL GSNVKKFKVG DQVCGVGSKT
     SSSHIIVDYD YIYYKPLNYS HSVSALIPSV YITSLHSLYG IGSLKSNESI LIHSAAGGVG
     ISSLDLLKSK QHQGYIFLTV GSKDKEEYLI NKYGSLITAI YSSRNKDYVY EIKNKLIELG
     VVEQHQQGVD LILNTLSSEY MDSNFQCLNL SGRIVDLSII HLTSNDYMTN NHYKFNMNYG
     NVYVEDFTSK LIKSYLKKII KMINSNKLEL SVPIIEYSNN QFKDAIEYIN QRKHIGKIIV
     NHNQDEFNRV YNNYQSNNNQ IILKHSYDIS KLNIGKNILL TGQTGIVLEI LKYLVKYSND
     SIENIIILSK SKLKWELELL INQSKFKKDN NIKFHFNQID IEDSNKVNQV LNQLELNENI
     TNIDSIIHFA FMNDIGDVQQ VDMNRLNNTH GAKTIGAINL HNQSINRSWN IKQFIMASSV
     VSILGSDQQC CYVSACSVID SLSKYRHSIG LPSLAINLGA ISSTGFVSRN NAIETMFKSS
     ILKLFSPQLV ISSLDLFIQN QHQYPNYCLS DFNFEILPST LTNQYHSKFD FEINIVKKSN
     QIKSFTGSND GDNNNEIIRS TILNKICELL SIDESKINED LQLTQYGMDS LVIVQLKNFI
     DNQLGHNIIT IQQLQNNKIN QSIEIILSAH NNNNKNNNNN NNINNNNKNN NNNNNKNNNN
     INNNINNNKN NNNNNNLVKK EQQSLDEFIK NEMKLNESII SRPYSIKNIL NKSNNSKSIF
     LTGSTGFLGA YLLTELIKMN NISKIYCLIR NNSKLTNPID VIINNLKKHQ LINMNKESPN
     QRLTKIINHT GNISNDKLSN IENSEYYKQI SEDQLIKIIP MIGDISKDKF GLTEQDYLKL
     SNECDIIINS AADLNLKSNY EESKTVNVNS VNQIVKLSVS NNSSQKLIVH FSSIAVFINH
     PFKDGEEFEE TNILPNFDTT PIGYIQCKVI SEKLLTNAAE SRGIPSIIIR PPDIFSNPIT
     GIGHSNDFVS LLLKTSKEIG YYPNIYKSIF TTPVTTIAKT TIDLIFNENS WNQNKSKPIS
     IYSLNGNSIE MKSIYKFLEN NYNCKEIDYQ EWIELVSKSN GMSSKRYSTF HIHDNQNLMV
     SNFKINSLFK MSNSTKELLT SIGSYNHQDW EINESIILKN INNNNN