ID   PKS34_DICDI             Reviewed;        3078 AA.
AC   Q54FN2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable polyketide synthase 34;
DE            Short=dipks34;
DE            EC=2.3.1.-;
GN   Name=pks34; ORFNames=DDB_G0290737;
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 pks33/pks34 in chromosome 5.
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DR   EMBL; AAFI02000169; EAL62074.1; -; Genomic_DNA.
DR   RefSeq; XP_635580.1; XM_630488.1.
DR   SMR; Q54FN2; -.
DR   STRING; 44689.DDB0235303; -.
DR   PaxDb; Q54FN2; -.
DR   PRIDE; Q54FN2; -.
DR   EnsemblProtists; EAL62074; EAL62074; DDB_G0290737.
DR   GeneID; 8627801; -.
DR   KEGG; ddi:DDB_G0290737; -.
DR   dictyBase; DDB_G0290737; pks34.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54FN2; -.
DR   OMA; HAYESQH; -.
DR   PhylomeDB; Q54FN2; -.
DR   PRO; PR:Q54FN2; -.
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; 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..3078
FT                   /note="Probable polyketide synthase 34"
FT                   /id="PRO_0000371394"
FT   DOMAIN          2541..2618
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          181..234
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          665..698
FT                   /note="Acyl/malonyl transferase"
FT   REGION          1375..1396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2617..2640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2739..2761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2621..2652
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        675
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2578
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3078 AA;  350410 MW;  3173FB11C0DE972D CRC64;
     MTENIHNNST YNNKLIRDRN DYDDVDGSGD VAVIGIGLRF PSGNLKESIS KPNQLFNELL
     NGLDGIVTTS ERWSDNYYLN GEIVSKFAGL LPLDEWKQFD PIFFAINPSN DNVSSIDPQQ
     RLLLKCVWEA LEDSGIDPIS LRGTNTSTFI GSSTIDYNDL QRSPLETQNN IFGSTTHSIA
     NRIGYCFDFR GENLTIDTAC SSSSNAINCG YNSIKSNKSN VSIVGGVNFI LDPHISKSFT
     KLDMLSPTGR CHTFSSDADG YVRSEGVGIV VLKKLKDAIK DSNNIYCVIK GSNSNIDGNF
     DKLNFYSPSK SSQYENIKLA IKSTNGQINE SDIDYCETHG TGTPTGDPIE LEGISRVFNN
     KASTTTLINN NKQVLVGSIK SNIGHTEACS GVASLIKCCL MFKNKLFLQN INFKEPNPLI
     NFKEWGLKVV TEPIKFNENK STVMLLNNFG VTGSNVCLIL SEFYGNQFSY NKSNSYHKIK
     IDNKFNEKKK YLIPLSSNSS TSLNNYKSSI IKHSNSSSTT TSFKEFVHNQ IKFKSTSLIQ
     KSVIIASDWN EFQDENNQIK LENSDNLISN ITVEKKKSPI TVMVLCGQGS QYNKMASSLY
     DNEPIFRESV NRFDKELFKY YGYSVLDKLR SIDDKDLISI HQPILAQPAN VIIQVSLYEL
     YKHWGVSADI IIGHSLGEIS SSYCSGIIDF QTLCYLTYHR SVAQNRTIGT GRMLSVNISS
     DEFINKYQST TKYESLEIAC YNSPTSIVIS GNEDLLNEIT NEFKSNDIFC TMLGLLSSFH
     TSSQQMIKDE VCSLNISSKQ PSIAVFSTVT TNLFNHQSSP FNADYVFNNI RQPVRFTQTI
     TNLYKHIESN DMGNEITFIE VSPHPTLQYY LNQMKSTQSS YFNNGKNITI YSPLNKKKND
     YNEFLKTISL LYVNNNFDIN FKSQLINNNN TNQLNNLPLY QWDDKEYFKI NSFHEKIKNE
     GPSIHSLGNN TDSPYPSYQT FIDIKKLPFQ WLKGHQVSDK FYYPGMGYVL NLLSIYPNQD
     ITIGSLEFKS PLVLTEGNNQ CLQTTIAPLS KNEFNIKSHY KDQKTNQWIL SSLGNFSLTK
     HNIENNEPIN IQSLKDKCNF TSISKQDLYE TIRIKTNLTY KGLFQGVKQC HIGSNCSLTI
     VSLNEIYNQK EYNHLLNNSI MDTFFNTAIL DTCLHGVLVA VTQPIVLDRI EAFKFYSSNY
     PSFNNNNNSN NNDTIKELYV YSEIRARTNS QTYSGSIKII LPNGTLLVDI GNVVCTIVGS
     NPDSTIICKP PSNEIYTPYL QSKDSMINKP EQFKHLYRVD EFSVKEEGNR FISKGLLPSL
     FYKHINKRCP SINLESLTTL EYDQFKQLYY DNSLANENLF KFIFEVLKKF QNNPNINNNN
     NNNNNNNNNN NNNSNGYNNY ENLYIRATKV MAKQLFPLKD DDSITDTPQS LFESGYLDEF
     YKNSNVIKPS NNLLSEIIVE TLKPILNEPI VFRILEAGGG TGSLSLLILE KICKLLNDNS
     TTSIINIEFT WSDVSASFFA EIKENFSSFT NHNNLNIIYR VLDLEKPLLD QDLKASYYDF
     VVMSNVMHVV KKLKPTLNEI HNILTPNGQL LFIEPPYKSF YFDSIFGCFS QWWPSSDSDI
     ELRPDRCCMK QEKWINLLNQ CNYRDTIMSG NDNLVFLIQT RKPTINEIIS EQSISLDQLN
     SFNNIILFSS NSNNIRNINS YKNDICSSSI QNLIRLNQEL KHKIVNISNY NEFQSWITNY
     QNKDDCNKTL IIFLKSIEST MNTFNFKEIT FEYIQINQLI LKLELSNNFK HLLLSLNSTT
     DNYLSSSIIG AARYFVEFPQ LDLLTLNYDN ISIENNQQLS LINYLINPNN NIQKEFTINN
     NKVYYERYCR RSNNIKSIFQ SKSFETNKDN LYIQLNSNLE YQLYSKKAKL NSNEVEIEVK
     ATGINYKDYL MYIGMIGSDL DIKYGKEYEI ENGIGIDNPN IGNDFSGIIT RLGNNVKKFK
     VGDQVCGIGS KASSSHVIVD FTSIYYKPLN YSHSVSASIP SIYITSLHSI YSIGNLKSNE
     SILIHSAAGG IGISSLDLLK SKQHQGYIFL TVSSKDKEEY LIKKYGSLIT AIYSSRNKNY
     VKDIKNKLME LGEVEQQGVD LILNTLSSEY MDSNFQCLNL SGRIVDLSIT HLTPNDYMTN
     NHFKFNMTYS NVEVVDFTSK LIKSYLKKII KMINSNKLEL SVPIIEYSNN QFKDAIEYIN
     QRKHIGKIIV NHNQDEFNRV YNNYQSNNNH IIMKHLYDIS KLNIGKNILL TGQTGIVLEI
     LKYLVKYSNH SIENIIILSK SKLKWELELL INQSKFKKDN NIKFHFNQID IEDSNKVNQV
     LNQLELNENI TNIDSIIHFA FMNDIGDVQQ VDMNRLNNTH GAKTIGAINL HNQSINRSWN
     IKQFIMASSV VSIFGSDQQC CYVSACSVID SLSKYRHSIG LPSLAINLGA ISSTGFVSRN
     NAIETMFKSS IFNLFSPQLV ISSLDLFIQN QHQYPNYCLS DFNFEVLPST LTNQYHSKFD
     FEINIVKKSN QMKSFTGGNG DNNEIIRSTI LNKISELLSI DESKINEDLQ LTQYGMDSLV
     IVQLKNFIDN QLGHNIITIQ QLQNNKINQS IEIIKSAHNN NNNNNNNNNN NNNNNNNNNN
     LVKKEQQSLD EFIKNETKLN ESIISRPYSI KNILNNNNNS KSIFLTGSTG FLGAYLLTEL
     IKMNNISKIY CLIRNNSKLT NPIDVIINNL KKHQLINMNK GSPNQRLNSN IESGDNSDNN
     SQISEDQLIK IIPTIGDISK DNFGLTEQDY LKLSNECDII INSAADLDLK SNYEESKTVN
     VNNVNQVIKL SVSNNSSQKL IVHFSSLAVF INHPFKDEED FEETNLVPSY NSTPIGYVQS
     KVISEKLLTN AAESRGIPSI IIRPPDIFSN PITGIGHSND FISLLIKSSK EIGYYPNIHK
     SVFTTPVTTI AKTTIDLIFN ENSWNQNKSK PISIYNFNGD SIEMKSFYRV LENSFKCKEI
     DFYEWIELVS KSNGKSSKRY STFHIHKNQN LLLTSFKINS LFKMSNSTKE LLISIGSYNH
     QDWEINESMI FNDIINNH