ID   PKS17_DICDI             Reviewed;        2604 AA.
AC   Q869X2; Q554C1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable polyketide synthase 17;
DE            Short=dipks17;
DE            EC=2.3.1.-;
GN   Name=pks17; ORFNames=DDB_G0275077;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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   [3]
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 pks16/pks17 in chromosome 2.
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DR   EMBL; AAFI02000013; EAL69819.1; -; Genomic_DNA.
DR   RefSeq; XP_643790.1; XM_638698.1.
DR   AlphaFoldDB; Q869X2; -.
DR   SMR; Q869X2; -.
DR   PaxDb; Q869X2; -.
DR   PRIDE; Q869X2; -.
DR   EnsemblProtists; EAL69819; EAL69819; DDB_G0275077.
DR   GeneID; 8619835; -.
DR   KEGG; ddi:DDB_G0275077; -.
DR   dictyBase; DDB_G0275077; pks17.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q869X2; -.
DR   PhylomeDB; Q869X2; -.
DR   Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-DDI-199220; Vitamin B5 (pantothenate) metabolism.
DR   Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR   PRO; PR:Q869X2; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
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; 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; IPR029063; SAM-dependent_MTases_sf.
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; 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; 2.
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   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2604
FT                   /note="Probable polyketide synthase 17"
FT                   /id="PRO_0000371382"
FT   DOMAIN          2507..2584
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          160..213
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          631..664
FT                   /note="Acyl/malonyl transferases"
FT   REGION          1357..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2581..2604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        179
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        641
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2544
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2604 AA;  291203 MW;  9471188B421EAC24 CRC64;
     MTFNNIKDEN NDDIAIIGMG FRFPGGGNNP YQFWNQLSNK MDGISKIPTE KWSRSFYEQK
     YINNEYGGVL KDEEWKNFDP LFFGISPKEA PIIDPQQRLL MTTLWEAFED ANIKPSTFRG
     SDTAVFIGMM NTDYQRCQFR DISYVNPYIT PGTAGSFISN RLSFSFDLRG PSMTLDTACS
     SSLNAVYLGC QAIANGDSKM AIVGGVNGIF DPCFSMTFSG LNMLGHKGQC RSFDAGADGY
     IRSEGGGVCI LKKYSDAIKD GDRIYCVIKG GSSNVDGYNA KTNIIQPSMK AQGENIEIAL
     KKSGVNPSDI YYIEAHGTGT PVGDPIEIEA ISRIFKDNHT PDAPLYIGSV KSNIGHLESA
     AGIASLIKVA LSLKNRSLVP NIHFEKPNPL IKFEDWNIRV VTDEIQFPIN KLINMGINCF
     GLSGSNCHMI LSEAPINYDE LLKTTNNNST SSSSNDDKKE YLIPFSANCN ISLDKYIEKL
     ISNQSIYKDT ILFKDFVKHQ TISKSNLIKR KVITASDWDD FLNKRNETTS TSSLTSTISA
     PASSTPVIYV FTGQGPQWRD MGKALYETES VFKDAIDHCD KLLANYFGYS ILQKLLSLES
     EDSPEIHHPI LAQPSIFLIQ VGLVALYKSF GISPSIVVGH SFGEIPSALF SDVISLETAV
     KIVYYRGLAQ NLTMGTGRLL SIGIGADAYL EKCALLYPEI EIACYNDPNS IVITGSEQDL
     LGAKSTLSAE GVFCAFLGTP CSFHSSKQEM IKEKIFKDLS DLPESNVPCV PFFSTITGSQ
     LSHKGFYNVQ YIYDNLRMPV EFTKAISNIF NFIEENESYK NAIFLEIGPH PTLGFYIPKC
     KPSNSTITSK PIIVSPLHKK KEELTQFKLA ISTLYCNGVE IDFASGQQLL PTSSSSGGGD
     ISSFKESTNK LPRYQWDFEE YWDEPNQSKM VKRGPSNNLL GHDQFAGNTL MELFIDIDKS
     AHQYLKGHKI KGKYLFPGSG YIDNILRQFN GQDITIFNLE FSNPFFLKDG VQHHLQTSIT
     PTTKGEFKVE FFIKDNRNST KWTKTSNGRI GLFKHNPKNN KLDIEKLKSQ CSFTTLTKSE
     VYNKLLLLSL PYGPTFQRVE SCSIGDGCSF FKLSMSPCSE FDKDFLNPSI IDCAFHGLLV
     LSEGPQEIVF DRLQDMKFYS SNVPSTRPQF IYAFAKFDKI EGNSTHGSLN IILEDGTLLI
     SIKNVKCTSL IRLKKQSIKY PSQNVYSHHW QSKDSPLTLI ENQLIEEKSS ESKINFEKLL
     NDKLFNYYLI RLLNQSIKSE FIEFDYKTST VDTLDIGSKN AKLLEKIQSI LNPIDSLDQS
     IDITSLKQAI IVKSSFKNEI KLVEKSIKRI VSLLKGGESE HFSPSNPSSP NDTPRNNSNN
     CSSKNNAASS DDADDDTNNE ETINQLNNEP FNFSNSQFIS NQNQLISKTI VNSFDRLINS
     IEIGEKKLIK IIDLSSIYQN YQLSKLLLLQ LNQLLINLSN NNNIEIEYTI PSNTKNIDSI
     TEETKSISNV LNIKYRSFDL QDDLESNGYL NSNYDLIITS LLLVSTNSID SNEVLSKLYK
     LLLPKGQLIL MEPPKGVLSF NLLFANDFKQ SLEIKSEQEI KSLIIYCGFT KIETNLNTKD
     DEEQQQPPPP SILIVQAEKR DIESMSLTFS SDPKSLNSSY SNCIFIVSKE QKENPTSYIQ
     EYFDITEFFC QNATIIEADD SELLTKTIES GVGKNDIIFF LVSLEELTIE NYKQVTMQYT
     LVNQILLRNN LSTRFALLTY DSQNGGKNYL GSSLIGTFRY FLEFRSLNIF SIDVDKDSID
     NLTLFLRLVD LSTIGDRETI VRNNKIFVQK IFKEPKLLSP SNNYEKNTNN LFLYSNSNLD
     FSFQSKEKLL HGCVEIKVMS TGINYKDSLF YRGLLPQEVF SKGDIYSPPF GLECAGYITR
     VAPSGVTRFK VGDQVVGFAS HSLSSHVTTH QNKIVLKPEN ISFNEAAAVC VVYATSYYSI
     FHIGAFIADK ESILVHSATG GVGLASLNLL KWKRNQLKKH GNSEISNDAS IYATVGSKEK
     IDYLQEKYGD LITAIYNSRD TEYCDEIKQQ SAQGGVDLIL NTLSGDYLSS NFRSLSQVGR
     IMDLSVTQLV ENDSLDFSNF KYHVGYNTID LDRATKYNSK IIRDILTEVF DAISDGSLEN
     IPVKVFPAIQ VKTAIEYINE RVHIGKIVVD FENFEQDILK PALQEKENPI QLNKVKKLEH
     TCDTLNNTIL ITGQTGIAVH ILKWIISGSV LNSNKSQQQV TDFIILSRSS LKWELENLIN
     QTKHKYGDRF RFHYKSVNIA DLNSTRTAID QVYSSCKNVS PIKSVLHFAT VYEYILPENI
     TQTVIDNTHN PKAVGAINLH NLSIEKDWKL ENFILFSSIG AIIGGSKQCA YSSANLVLDS
     LSNYRKSIGL ASTSINWGGL DAGGVAATDK SVASFLEGQG ILLVSLSKIL GCLDSVFQPS
     NSHLSNFMLS SFNIDNLLSS APQMKRKMDH HLTNYKTSSA SSDDSLGDSG STQAKVISTI
     SELLSIHPSK LNLDTRLKDY GIDSLLTVQL KNWIDKEFTK NLFTHLQLSS SSINSIIQRI
     SSKSTSTSTP NPTNTSKQTA TKKT