ID   PKS5_DICDI              Reviewed;        2512 AA.
AC   Q86JI5; Q55AY9;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable polyketide synthase 5;
DE            Short=dipks5;
DE            EC=2.3.1.-;
GN   Name=pks5; ORFNames=DDB_G0271520;
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).
RN   [4]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA   Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA   Ivens A., Martinez J.L., Escalante R.;
RT   "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT   and specific effects from PAO1 and PA14 strains.";
RL   BMC Microbiol. 8:109-109(2008).
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   -!- INDUCTION: Up-regulated by P.aeruginosa, PAO1 strain and PA14 strain
CC       infection. {ECO:0000269|PubMed:18590548}.
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 quintuplet pks5/pks6/pks7/pks8/pks9
CC       in chromosome 2.
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DR   EMBL; AAFI02000006; EAL71624.1; -; Genomic_DNA.
DR   RefSeq; XP_645557.1; XM_640465.1.
DR   AlphaFoldDB; Q86JI5; -.
DR   SMR; Q86JI5; -.
DR   STRING; 44689.DDB0235300; -.
DR   PaxDb; Q86JI5; -.
DR   EnsemblProtists; EAL71624; EAL71624; DDB_G0271520.
DR   GeneID; 8618014; -.
DR   KEGG; ddi:DDB_G0271520; -.
DR   dictyBase; DDB_G0271520; pks5.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q86JI5; -.
DR   PhylomeDB; Q86JI5; -.
DR   PRO; PR:Q86JI5; -.
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; 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; 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; 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; 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   2: Evidence at transcript level;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2512
FT                   /note="Probable polyketide synthase 5"
FT                   /id="PRO_0000376880"
FT   DOMAIN          2430..2507
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          168..221
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          638..671
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        187
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        648
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2467
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2512 AA;  285270 MW;  1920B530724E3CE1 CRC64;
     MDMKLNDIEN ENFINQMKGV AIVGIGFRIP SGNSENSISS PDDLFNNLKN GFDGVSSTSE
     RWSDNYHKLG EISSPNAGLL PLNEWKSFDP LFFGINPSDA HHIDPQQRLL LKCTWEALED
     ASIDPISIRG TNTSVFIGSS TIDYLHANKH PDLILKNAIG FSPSTLSNRI SYCFDIHGPS
     LSIDTACSSS MNAVTQGYHS ILNGTSNMSI VGGVNFVIDV ETIKGFSYLN MLSKTHGKCK
     AFDESGDGFT RGECAGVVVL KKLDDAIRDG NRIYCIINGI SSNIDGNGIA DKANFYSPSK
     QSQFNNINLA FKSTNGKISV NDIQYIEAHG TGTKTGDPIE TEAISMAFKN RDKSTPILIG
     SIKSNIGHCE AGSGVVSLIK CCLMFKYQCF LPNIHFKNPN PLIKFNEWNL KVVTSPIPFN
     RNNEKSVSMM INNFGVTGSN CCLLISEFKK QDYESYENNI GSINKNILVP FSANSPKSLD
     QYQSKIKNII NNQFNFIDFA NNQIYSKSNY LYQRSVVIAN NSNDLVNKIL NKKHIQTKNP
     IISNMSFKGK NPITIFVFSG QGSQYPKMAL ELYNNEVIFK KSIDLIDSKL SKYYGYSVLE
     KLRSIGDDDT TSIHDPTIAQ PAMCMFSVSL FELYKHWGVN PSFILGHSLG EIPTSYCSGM
     IDLDTFCYTV YQRSIAQTKT HGNGRMLSIN ISDEEFKSMY SQKYPQIEIA CYNSPQSIVV
     AGNESILNEI SKELKEKEIF TAMLGSLSSF HTSSQQCTKD SILQLNIESK KSKVPTFSTV
     TTNLFNESDP FNSQYVYDNI INPVKFTQTI SNIYKHIESN QLDNDIVFIE IAPHPTLSFY
     IKQMVPSSLN ESVSVYSALH KKKNDVEEFQ QTISNLYCQN GYNINFKCQF NNKKSNQKIN
     LPLYQWDDEL YFAQTQVLEQ HRKEGPPIDH LGLSNSYYSP FKNSYRTFID IKNKPFQYLK
     GHMVKGKYYF PGCGYIDNII QLYKNQDIFI SFIEFKTPLI LIEGINQCLQ TNIQQTGKSE
     YRAQFHFKDQ KSNEWIQSSN ANFQLLDHTI EMPPKYNIEE IIKNKCTLAR LTKNEIYTHI
     KSKTGLNYTA MFQGATECYI GVDCTLSVVS IESQTNSFLN IPILDSVFHG NISLINDQCQ
     IVFDKVHGLK YYSSNIPNDY KDKSVYVYAK LKSKTSDSYS ASFTVLLSDG TVVYEIDEAF
     SKSLIPIKEL LKIEYPNDEL FSINLQPKDS PIPAPSTFKS LIYENDRFNA EPPMVENLFQ
     YISTIFYKNI INRCPEINID IIKSLSIDEI ISNFSKISKH ERLFKYVFET IKENGILNSL
     EEKDDTYFVF NEVLIKSSRV ISKLLFPLEN DNDNEDTPQL LFQNGLMDKV YKCRYLKNKN
     QMIAHIIKHS IKEIINNNII IRILEFGGGT ASLSVEVIEE IVTLLQENPN YQVEIEYTWS
     DISPAFIVDT KNKINKIIKG AGITNGLNVI YHPLTIDESL VELQSIKPSY YDFVIMSNVL
     HVVKDIKQAV EQMYQLLIPN GQLLFVEPPY KSIICDSLFG SFEQWWAFTD TDIRKDHCCL
     SQDGWYKLLK WSNFESIEMS TESKFMGSVI QAQKPSFTSL INQQPKYDNI IIFGNNCPNF
     IDNIKPFSNF NEFIQIETIQ EFDQLINKST ITNDSIIYFI KSINQLSLDN YKQATLEYIE
     INQKLLQINS LCKHVLIVND SRKTNYLASS IVGAARYFDE FQQLKLHTLD FDYDSTQNYL
     ISKNNKMVQF INNLIDSKTN VHKEMIIINN KVYYEIVQKE KNLKLKYNSE SFEQQDNLMC
     SLSPNLEYQL QSKQIKLRDN QVEVKTIATG INNKDYLVYS GLEGSVNSNT PQFGYEFSGI
     ITRVGNNVKD YKVGDNVFGL SNSCTSSNII VNHERIQIKP SNISHIEAAS IPIDYLTSFM
     SLFNVGCLNI EDNESILIHL GSDSFGLSTF EILKWKGFKS NLFVTVNSDE IKQYLLNNYG
     DLITAIYSNT DKGYVSQIKN KLIEQGSNDN GVDLILNTLP SDFMDSNFQL LAINGRIIDL
     SNDHLNQSEY MKNVNFTLNR GYHNFDLMSQ RNSRINRSLL TISKAIENGE LKLIPIKEFS
     NSDINDAIEF IIEENRIDKI VVSHDHEVYQ ELYAKFSNEN DFSILKSNYQ INSNNLGKNI
     LITGQSGIIL EILKWIIKYS NINTIENVII LSRSSLKWEL ELLINQTKLS NNNIKFHFKS
     VDVGDSEQVD NAINEILNEN QEIINIHSIF HFAFTQIACK VQEINMKHLD ISHGAKTMGA
     INLHNQSIKR NWKLINFVIS SSIASLVGST DQCSYVCANA LLDSFSKYRV SLGLPSTSIN
     LGAIESTGFV SKNESISVFL DGSGIIPTPI NQVLGLLDLQ IQNPGKFTNS MVAKFNPLNF
     SNNEQINLLL KMDYIFNLHS NGYTKVKESA GSKNVDELFI KKISDLFSID ESKINKDIRL
     IDYGADSLVI VQLKNWVDQE IGFNLITIQQ LQNNTINVSI KIILNFLKKI NK