ID   PKS38_DICDI             Reviewed;        3133 AA.
AC   Q54FD2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable polyketide synthase 38;
DE            Short=dipks38;
DE            EC=2.3.1.-;
GN   Name=pks38; ORFNames=DDB_G0290937;
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 pks38/pks39 in chromosome 5.
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DR   EMBL; AAFI02000172; EAL61984.1; -; Genomic_DNA.
DR   RefSeq; XP_635490.1; XM_630398.1.
DR   SMR; Q54FD2; -.
DR   STRING; 44689.DDB0235304; -.
DR   PaxDb; Q54FD2; -.
DR   EnsemblProtists; EAL61984; EAL61984; DDB_G0290937.
DR   GeneID; 8627906; -.
DR   KEGG; ddi:DDB_G0290937; -.
DR   dictyBase; DDB_G0290937; pks38.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54FD2; -.
DR   OMA; PAWKLYT; -.
DR   PhylomeDB; Q54FD2; -.
DR   PRO; PR:Q54FD2; -.
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; 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   Coiled coil; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..3133
FT                   /note="Probable polyketide synthase 38"
FT                   /id="PRO_0000371395"
FT   DOMAIN          2562..2639
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          162..215
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          647..680
FT                   /note="Acyl/malonyl transferase"
FT   REGION          1370..1408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2691..2715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2794..2817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2649..2711
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        181
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        657
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2599
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3133 AA;  357196 MW;  AD86A31ED1B71E31 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 KLSQFENIKL
     AIKSTNGQIN ESDIDYCETH GTGTPTGDPI ELEGISRAFN NKASTTNNNK QVLVGSFKSN
     IGHTEACSGV ASLIKCCLMF KNKLFLQNIN FKEPNPLINF KEWGLKVVTE PIKFNENKPT
     VMLINNFGIT GSNVCLILSE FSGYQFGYSK SNDYQKMEID NKFNEKKKYL IPLSSNSSTS
     LDNYKLSIIK HLNSRSSSSS TTTSFEEFVY NQIKFKSTSL IQKSVIIASD WNEFQDENNQ
     IKLENSDNLI SNITVEKKKS PIIVMVLCGQ GSQYNKMALS LYDNEPIFRE SVNRFDKELF
     KYYGYSVLDK LRSIDDKDLI SIHQSILAQP ATVIIQVSLY ELYKHRGVSA DIIIGHSLGE
     ISSAYCSGMI DFQTLCYLTY HRSVAQNRTS GTGKMLSVNI SSDEFINSYQ STTKYESLEI
     ACYNSPTSIV IAGKEDLLNE ITKDFKTNDI FCAMLGSLSS FHTSSQQMIK DEVCSLNISS
     KQSSIAIFST VTTNLFNDET SPFDADYVFD NIRQPVRFTQ TITNLYKYFE SNDMGNEITF
     IEVSPHPTLQ FYLNQMKSTQ SSYFNSGKNI TIYSPLNKKK NDYNEFLKTI SLLYVNNNLN
     INFKSQLIDN NNNYTNQFNN LPLYQWDDKE YFKISWFQEK IKNEGPSIHS LGNNTDSPYP
     SYQTFIDIKK SPFQWLKGHQ VSDKFYYPGM GYVHNLLSIY PNQDITISSL EFKSPLILTE
     GNRQCLQTTI APLSKNEFNI KSHYKDQKTN QWILTSLGNF SLSKHNIENN EPINIRALKD
     KCNFTCISKQ DLYETVRIKT NLTYKGLFQG VKQCYIGNNC SLAIVSLNEI YNQKEYNHLI
     NNSNMNTLFN TAILDTCLHG VLGVVTQPVV LDRIEGFKFY SSNTPSFNNN STNSNNDTIN
     ELYVYSENKA RINSKTYSGS IKIILPNGTL LIDIGNVVCT IVASNPDSTI ICEPPSNKIY
     TPYLQSKDSV IKNPEQFKHL YRVDEFSFKN EENQFISIGL LLSLFYKHIN NRCPSINLES
     LETLEYDQFK QLYYNSSRNE NLFKFIFENL KNYQNIMYSN SFNKTILFNN NNNNNNNNNN
     NNNNNNNNNN NNNNNNNNNN NNDNDNDNNC YNYENFYIRT TKIMAKQLFP LKDDDSITDT
     PQSLFESGYL DYHYKNSKIV QPLNNLLGEI IVETLKPILN EPIVFRILEA GGGTGSLSLL
     ILEKICKLLN ENNSTSIIDI EFTWSDISAS FFAEIKEKFS SFTNHNSLNI IYRVLDLEKP
     LLDQDLKASY YDFVVMSNVM HVVKKLKPTL NEIHNILAPN GQLLFVEPPY KSFFIDSIFG
     CFSQWWPSSD SDIELRPDRC CMEQEKWISL LNQCTYRDTV LYGNDKLLFL IQTRKPTINE
     IISEQSISLD QLNSFNNIIL FSSNNNNDNN NNSNNYYNNR NSYSSSSIQN LIRLNQELKH
     KIININNYNE FQSWITNNQN KDNCGNKTLI IFLKSIESIM NTSNFKEITF EYIQINQLIL
     KLELSNSFKH LLLSLNSTTD NYLSSSIVGA ARYFVEFPQL DLYILNYDNI SIENNQQLLS
     LINYLIDSNN NIQKEFTIIN NKVYYERYCR RSNNIKSKLQ SKSFETNKDN LFIQLNSNLE
     YQLYSKKDEL NSNEVEIEIK ATSINYKDYL MYIGMIGTDI DIKYGKEYEI ENGIGIDNPK
     IGNDFSGIIT RLGCNVKDFK VGDQVCGVGS KTNSSHIIVD YNYIYYKPLN YSYSVSASIP
     SVYITSLHSI YNIGNLKSNE SILIHSAAGG IGISSLDLLK SKQHQGYIFL TVGSKDKEEY
     LIKKYGSLIT AIYSSRNKNY VKDIKNKLIE LGEVEQHQQQ GVDLILNTLS SEFMDSNFQC
     LNLSGRIVDL SITHLTPNDY MTNNHYKFNV GYFNVEVIDF PGKLIKSYIK KIIKMINSNK
     LEPSVPIIEY SNNQFKDAIE YINQRKHIGK IIVNHNQDEF NRIYNIYQNN NNQIMKHSYD
     ISKLNIGKNI LLTGQTGIVL EILKYLVKYS NHSIENIIIL SKSKLKWELE LLINQTKFKK
     DNIIKFHFNQ IDIEDSTKVN QVLNQLELNE NITNIDSIIH FAFMNDICDV QKVDMNRLNI
     THGAKTIGAI NLHNQSINRS WNIKQFIMAS SVVSIFGSDK QCCYVSACNV IDSLSKYRHS
     IGLPSLAINL GAISSTGFVS RNNAIETMLK STLSNLFSPQ LVISSLDLFI QNQHQYPNYC
     LSDFNFEVLP STLTNQHHSK FDFEINIVKK SNQIKSFSGD DNNNEIIRST ILNKISEILS
     IDESKINEDL QLSQYGMDSL VIVQLKNFVD NQLGHNIITI QQLQNNKINQ SIEIIKSAHN
     KNKNNNNNNN NNSNHHDNIK KEQQSLDEFI KNETKLNESI ISRPYSIKNI LNNNNNNNNN
     NNNNNNNNNN NNNNNNNNNC QSIFLTGSTG FLGAYLLIEL IKVNNISKIY CLIRNNSKLT
     NPIDVIINNL KKHQLIDMNK ESPKRKTKII NHTGNISNDK LNSSNSNSDN SNNNNNQINE
     DQLIKIIPII GDISKDKFGL TEQDYLKLSN ECDIIINSAA DINLKSNYEE SKTVNVNSVN
     QIIKLSVSNN SSQKLIVHFS SLAVFINHPF KDEEDFEETN SVPSFNSTPI GYIQSKVISE
     KLITNAAESR GIPSIIIRPP DIFSNPITGI GHSNDFISLL IKASKEIGYY PNIHKSIFST
     PVTTIAKTTI DLIFNENSWN QNKSKPISIY NFNGNSMEMK SFYRVLENNF KCKEIDFDEW
     IELVSKSNGK SSKRYSTFHI HKNQNLLLTT FTINSLLKMS NSTKELLTSI GSYNHQDWEI
     NESMILNDII NNH