ID   PKS39_DICDI             Reviewed;        3108 AA.
AC   Q54FC8;
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 39;
DE            Short=dipks39;
DE            EC=2.3.1.-;
GN   Name=pks39; ORFNames=DDB_G0290943;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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 pks38/pks39 in chromosome 5.
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DR   EMBL; AAFI02000172; EAL61987.1; -; Genomic_DNA.
DR   RefSeq; XP_635494.1; XM_630402.1.
DR   SMR; Q54FC8; -.
DR   STRING; 44689.DDB0237714; -.
DR   PaxDb; Q54FC8; -.
DR   PRIDE; Q54FC8; -.
DR   EnsemblProtists; EAL61987; EAL61987; DDB_G0290943.
DR   GeneID; 8627910; -.
DR   KEGG; ddi:DDB_G0290943; -.
DR   dictyBase; DDB_G0290943; pks39.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54FC8; -.
DR   OMA; LRPQWRN; -.
DR   PhylomeDB; Q54FC8; -.
DR   PRO; PR:Q54FC8; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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; 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; 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   Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..3108
FT                   /note="Probable polyketide synthase 39"
FT                   /id="PRO_0000371396"
FT   TRANSMEM        2702..2722
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2566..2643
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          162..215
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          643..676
FT                   /note="Acyl/malonyl transferase"
FT   REGION          1375..1435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        181
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        653
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2603
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3108 AA;  353866 MW;  73CE3B06A40C3448 CRC64;
     MTENIDKNDD DVAVIGIGLR FPSGNLKESI SKPNQLFNEL LNGLDGIVTT SERWSDNYYL
     NGEVVSKFAG LLPLDEWKQF DPIFFAINPS YDNVSSIDPQ QRLLLKCVWE ALEDSGIDPI
     SLRGTNTSTF IGSSTIDYND LQKSPFETQN NIFGSTTHSI ANRIGFSFDF RGENLTIDTA
     CSSSSNAINC GYNSIKSNKS NVSIVGGVNF ILNPYISKSF TQLDMLSPTG KCHTFSSDAD
     GFVRSEGVGI VVLKKLKDAI KDSNNIYCVI KGSSSNIDGN FDKLNFYSPS KLSQCENIKL
     AIKSTNGQIN ESDIDYCETH GTGTPTGDPI ELEGISRAFN NKASTTNNNK QVLVGSFKSN
     IGHTEACSGV ASLIKCCLMF KNKLFLQNIN FKEPNPLINF KEWGLKVVTE PIKFNENKPT
     VMLINNFGIT GSNVCLILSE FSGNSKSNDY QKMEIDNKFN EKKKYLIPLS SNSSTSLNNY
     KLSIIKHLNS RSSSSSTTTS FEEFVYNQIK FKSTSLIQKS VIIASDWNEF QDENNQIKLE
     NSDNLISNIT VEKKKSPIIV MVLCGQGSQY NKMALSLYDN EPIFREYVNR FDKELFKYYG
     YSVLDKLRSI EDKDLISIHQ PILAQPATVI IQVSLYELYK HWGVSADIII GHSLGEISSA
     YCSGMIDFQT LCYLTYHRSV AQNRTTGTGK MLSVNISSDE FINSYQSTTK YESLEIACYN
     SPTSIVIAGK EDLLNEIIKD FKSNDIFCAM LGSLSSFHTS SQQMIKDEVC SLNISSKQPS
     IAIFSTVTTN LFNHQSSPFD ADYVFDNIRQ PVRFTQTITN LYKYAESNDM GNEITFIEVS
     PHPTLQFYLN QMNSTQSSYF NSGKNITIYS PLNKKKNDYN EFLKTISLLY VNNNLNINFK
     SQLINNNNNN NNNNYTNLFN NLPLYQWDDK EYFKITSFHE KIKSEGPSIH SLGNNTDSPY
     PSYQTFIDIK KSPFQWLKGH QVSDKFYYPG MGHVHNLLSI YPNQDITISS LEFKSPLVLA
     EGNRQCLQTS VTPLSKNEFN IKSHYKDQKT NQWILTSLGN FSLFKHNIIE NNQPINIQTL
     KDKCNFTSIS KQDLYETIRI KTNLTYKGLF QGVKQCHIGN NCSLAIVSLN EIYIQKEYNH
     LINNSNMNTL FNTAILDTCL HGVLCAVTQP VVLDRIEGFN FYSSNIPSSL NYRNNNNNNN
     NINNNNNNNN NSNNTINEFY VYSEIRARTN FQTYSGSIKI ILPNGTLLVD IGNVVCTIAA
     SNPDSSLICK PNYIYTPHLQ SKDSIINKPE QFKHLHRVNE FSFKNEENLF ISNRLLLSLF
     YKHINNRCPS INLESLETLE YDQFKQLYYN SLVNENLFKF IFEILKKYQN IPNINNNNNN
     NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNEKLYI
     KTTKIMAKQL FPLKDDDSIT DTPQSLFESG YLDVFYKNSI VVQPLNSLLS EIIVETLKPI
     LNEPIVFRIL EAGGGTGSLS LLILEKICKL LNENNSTTSI IDIEFTWSDI SASFFAEIKE
     KFSSFTNHNS LNIIYRVLDL DKPLLDQDLK ASYYDFVVMS NVMHVVKKLK PTLNEIHNIL
     APNGQLLFVE PPYKSFFIDS IFGCFSQWWP SSDSDIELRP DRCCMKQEKW INLLNQCNYR
     DTIMSGNDNL LFLVQTRKPT INEIISEQSI SLDQLKSFNN IILFSSNNKN NKNDSFSIIQ
     NLITLNQELK HKIININNYN EFQSWITNNQ NIDNKTLIIF LKSIDSTVNT SNFKETTFEY
     IQINQLILKL ELSNNFKHLL LSLNSTTDNY LTSSIVGAAR YFIEFPQLDL LTLNYDNVSI
     ENNQQLLSLI NYLINSNNNI QKEFTINNNI VYYERFCKRL NNIKSKFQSK SFETNKDNLY
     IQLNSNLEYQ LYSKKDELNS NEVEIEIKAT GINYKDYLLH IGMIGTNLEI KYGKEIENGI
     GFDNPKIGND FSGIITRLGC NVKEFKVGDQ VCGFGSKTNS SHIIVDSDSI YYKPLYYSHS
     VSASIPSIYI TSLHSIYGIG NLKSNESILI HSAAGGVGLS SLDLLKSKQH QGYIFLTVGS
     KDKEEYLINK YGSLITAIYS SRNKNYVYEI KNKLIELGEV EQHQQGVDLI LNTLSSEFMS
     PNFQCLNLSG RIVDLSITHL TPNDYMTNSH YKFNMGYNNV NVEDFPGKLI KSYLKKIIEM
     INSNELELSV PIIEYSNNQF KDAIEYINQR KHIGKIIVNH SQDEFNRVYN NYQNNNNQII
     MKHSYDISKL NIGKNIILTG QTGIVLEILK YLVKYSNHSI ENIIILSKSK LKWELELLIN
     QTKFKKDNII KFHFNQIDIE DSNKVNQALN QLELNENITN IDSIIHFAFM NDIGDVQQVD
     MNRLNNAHGA KTIGAINLHN QSINRSWNIK QFIMASSVAS IVGSEQQCCY VSACNVIDSL
     SKYRHSIGLP SLAINLGTIS STGFITRNNT IETMLKSSIL NFLSPQLVIS SLDLFIQNQH
     QYPNYCMSDF KFKIIPSTNQ YFSKFDFEIN IVKKSNQIKS FFGGDGNNEI IHSTILNKIS
     ELLSIDKSKI NEDLQLTQYG TDSLVIVQLK NFIDNQLGHN IITIQQLQNN KINQSIEIIK
     SALNKNNNIY NNKKNNNNNL VKKEQQSLDE FIKNETKLNE SIISRPYSIK KILNNNNNSK
     SIFLTGSTGF LGAYLLMELI KMNNISKIYC LIRNNSKLTN PIDVIINNLK KHQLIDMNKE
     SPKRKTKIIN HTGNISNDKL NSSDNSNNNN NQINEDQLIK IIPMIGDISK DKFGLTEQDY
     LKLSNECDII INSAADLNLK SNYEESKTIN VNNVNQVIKL SVSNNSSQKL IVHFSSLAVF
     INHPFKDEED FEETNIVPNF NSTPIGYIQS KVISEKLLTN AAESRGIPSI IIRPPDIFSN
     PITGIGHSND FLSLLIKASK DIGYYPNIHK SIFSTPVTTI AKTTIDLIFN ENSWNQNKSK
     PISIYNFNGN SMEFKSFYRV LENNFKCKEI DFDEWIELVS KSNGKSSKRY STFHIHKNQN
     LLLTTFTINS LFKMSNSTKE LLISIGSYNH QDWEINESMI LNDIINNH