ID   PKS10_DICDI             Reviewed;        2485 AA.
AC   B0G103; Q86AD4; Q86JF0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable polyketide synthase 10;
DE            Short=dipks10;
DE            EC=2.3.1.-;
GN   Name=pks10; ORFNames=DDB_G0271662;
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 in chromosome 2.
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DR   EMBL; AAFI02000006; EDR41109.1; -; Genomic_DNA.
DR   RefSeq; XP_001732967.1; XM_001732915.1.
DR   AlphaFoldDB; B0G103; -.
DR   SMR; B0G103; -.
DR   PaxDb; B0G103; -.
DR   EnsemblProtists; EDR41109; EDR41109; DDB_G0271662.
DR   GeneID; 8618074; -.
DR   KEGG; ddi:DDB_G0271662; -.
DR   dictyBase; DDB_G0271662; pks10.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; B0G103; -.
DR   PhylomeDB; B0G103; -.
DR   PRO; PR:B0G103; -.
DR   Proteomes; UP000002195; Chromosome 2.
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   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; 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; 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; PF08242; Methyltransf_12; 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; 1.
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..2485
FT                   /note="Probable polyketide synthase 10"
FT                   /id="PRO_0000376885"
FT   DOMAIN          2410..2485
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          165..218
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          636..669
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        184
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        646
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2447
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2485 AA;  283234 MW;  ADB1B3C91F20D464 CRC64;
     MYLEKYQEDD IAIIGVGLRL PGEESGGGVV GELLNDSPQN FWNNLKKGFN GISKTNERWS
     ENYSKLGEIS NGYAGVLPLE ELKSFDPLFF GISPSEASTI DPQQRLLLKT TWESLEDAGI
     DHQSIRGSDC SVFIGSSTTE YRESIVNINE QYLNIFGTYA HGIANRISYC FDLRGESVTL
     DTACASSGTA ISMGAQCIKN GKSKLSIVGG VNLIVDTTNI KAFSYLNMLS TSGVCRPFDI
     GADGLLRGEG VGTIVLKSLK DSIRDGNKIY CIIKGSSYNV DGNGNSDKQN FYAPSSISQS
     DNIKLAIKST NGSITCDDID YFECHGTGTP TGDPIETKGI SMAFNRSKQN PLLIGSLKGS
     SGHSEAASGV IGVIKCCLIF KNKSLVPCVN FSKPNPQIKF EEWNLKVVTE PIPFTSLPSR
     KLNNKPISIA INNFGVTGAN CCIILSEFIN NNTNDNLKQI NKSFLIPFSA NSVKSLENYK
     LKLNSIINEN DYYLNNSAIF NGFVNNQIYN KSKSLSQRSV YVASNLNELV DGKVNFKTSN
     SKSSNFSILK KKPIVLFVFS GQGSQYNTMF DQLYNDEIIF KESIDRIDNS LFKYYGYSVF
     EKFKSSNLNS IHEPLIAQAA ISMLNISLFE LYKHWGIEAS FIVGHSLGEI SAAHCSGMID
     LETLCYIIYH RSIAQIKTHG NGRMLSINQS SDEYISKYSS KYADLEIACY NSQNSIVVAG
     NEHKLNQLFN ELKENNEFAT MIASQSSFHT SNQCITKDDI FKLQFTANLP LIPIFSTVTT
     NLFDNSTLFN SSYIYDNIIC PVRFEQTISN FYKHIDDDND KSDVEVVIIE LAPHPTLSYY
     LKQMKPVIEN KDIKVNVYSA LHKLKNSTKE FQKVISQLYC DNGININFKC QLENQVNMYD
     TIFSLPNYQW DDQKYWKVDY THSRSYINGP PITILGNESY NSPYLSRETY IDIKRNPFKY
     LNGHQIKMKI YFPGMGYIDN LLKLFKNNHK NIIIDQIEFI APLILNEGIN QCVQTNVNQI
     EINEYSLNCY YKDIKSNEWV KTCIGNFHIS NNLFTQQRNY NINQLINEKC NYSLIERDDL
     YDMIKIKTGL NYSGDFKGIN KCYIGNSCSL SEVSMNLPDN LPDKESFFNC TILDSCTHGF
     LVLIDYQCQL VFHKVEGLRY YNSNIPTDRN KHKNIYVYSI LNQILNDSFH SSVIIMLEDG
     TVLIEIDNLI SKSLTPIQDP LKIEYPMNEL FSTHLQPKDS PFPLISMTFK SKFKNINEIK
     NEFMLNCCKN FISNQFLSNI INRTNIKLNE IKTLTIDQLV KLYCLYNNNE RLFRFVFETI
     KKYDYNSNHS NNENEMVLKD DGIYQVLDTS IKVISKLLFP YENDKEDPIT ETPTSLFENG
     LLDKFYGTNN FMTTTIQRNL ITDIIINSLK PILNQKLVIR IVELGGGVCS FTVDFLEKLD
     KLLKENPFHE IEIEFTWSDI SSSFIPEAKK KLEPFSNNIN IVYRSIDIEK EFKKQGLKHS
     YFDFIILTNV LHVVKNIGNS LDQLYKILSP NGQILLIEPY VSIVNDSIFG SFSQWWSFED
     TEIRKTNCCM EPNSWLQVFK NHNFKNTNSY EEDGSCCYVI HSQKPPLLYG LNELKYTQSP
     NQIIIYGNEN ENENENENYT IKFNKSVIKI SNIDQFNQSI LNSQINNETI IYFTKSINQL
     DVNNFKFVTF EYIQINKLLL KYKLKSKHVL ITLNSRDSNY LSASLVGAKR YFEEYPQLSL
     KAIDFDLQSL EEIKDIQSLL IELLDENKNT QNDYIIKNCQ VYYERVKKEI ISKSKFISNS
     FENNDSLITQ LIDSEYKLTS NKPIFKVKEK EEGEEEVEIK VLSTTIGNVN DGDNFGEFSG
     IITRVCSNSN FKIGEKVYGF GYNTTSSHIV VNGDWIYYKP LNISNNNAAS IPYKYLEVLY
     GLYNIGELDE NENILIHLNN NINNNNNNIS TLNILKWKGH KGLIYVTVDS NEMEIYVNDN
     FGGFISGVFI LILKCLNSTS RIINFNYLNN NNNDNNDLEF FYKYCRKLNI GYHFIDLKKL
     IPIRRRGRII KDLFKEISKA IENNEINLLP IIDYSNLNIN HAIQMVKNEK NMVHTIVIEN
     NEDVLENLLK EHSNNSTYSI IKSDYKISEN HLGKNLIITG QIGVALEVLK WICKYSKGVE
     NIIILSKSLI KWELKLLIDK TYNSKENNQI KFHFNTIDIS NSNELTNTLN QLLKDTNIDN
     IDSIFHYAFT KVVSEVEDID LNQLNLSHGA KTMGAINLHN ESVNRCWNLK NFINASSTVT
     LAGSPGQCTY VCANSVLDSL SRYRKSIGLP SICSYYGSIK SGIVLRSESI ATSLEKQGYV
     HVSMNKFLGA LDLQIQNPNL STNLIVSNFN FKLFKNNPQH SIIDKFEHQI NENNSKLEIS
     TNNNPSTSTE SNKGIDGLLL SKVSELLSIN ETNFNADITL IDYGADSLIT SQLKNFIEKE
     FSLSVTSQQL QRNSINQLIK FLNKK