ID   PKS7_DICDI              Reviewed;        2513 AA.
AC   B0G100; Q86AE6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable polyketide synthase 7;
DE            Short=dipks7;
DE            EC=2.3.1.-;
GN   Name=pks7; ORFNames=DDB_G0271614;
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 quintuplet pks5/pks6/pks7/pks8/pks9
CC       in chromosome 2.
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DR   EMBL; AAFI02000006; EDR41105.1; -; Genomic_DNA.
DR   RefSeq; XP_001732963.1; XM_001732911.1.
DR   AlphaFoldDB; B0G100; -.
DR   SMR; B0G100; -.
DR   PaxDb; B0G100; -.
DR   EnsemblProtists; EDR41105; EDR41105; DDB_G0271614.
DR   GeneID; 8618017; -.
DR   KEGG; ddi:DDB_G0271614; -.
DR   dictyBase; DDB_G0271614; pks7.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; B0G100; -.
DR   PhylomeDB; B0G100; -.
DR   PRO; PR:B0G100; -.
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; 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   3: Inferred from homology;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2513
FT                   /note="Probable polyketide synthase 7"
FT                   /id="PRO_0000376882"
FT   DOMAIN          2426..2503
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          162..215
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          632..665
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        181
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        642
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2463
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2513 AA;  285227 MW;  AA7C4930BB9B5205 CRC64;
     MNNFKNINLI EKGVAIVGIG FRIPSGNNEN SISSPDDLFN NLKNGFDGVS STSERWSDNF
     HKLGEISSPN AGLLPFNECK SFDPLFFGIN PSEAPLIDPQ QRLLLKCTWE ALEDASIDPI
     SIRGTNTSVF IGSSNIDYLH TNKHQDSVLK NVIAQSTCAI SNRISYCFDF NGPSLSIDTA
     CSSSLNAISQ GYHSILNGTS DISIVGGVNL ILDVETTKAY SYLSMLSKTH GKCKAFDESG
     DGFTRGECAG VVVLKNLQDA VKDGNRIYCV INGSSSNVDG NGNMDKVNFY SPSKQSQFNN
     INSAFKSTNE KLSVNEIQYI EAHGTGTKTG DPIETEAISM AFKNRDKSTP ILIGSIKSNI
     GHCEAGSGVA SLIKCCLMFK YQCFLPNIHF KNPNPLIKFN EWNLKVVTSP IPFNRKNEKP
     VSMMINNFGV TGSNCCLLIS EFKKQDYEPY ENNYKSNNKN ILIPFSANSS NSLNQYQSKF
     KNIINNQFNF IDFTANQIYS KSNYLCQRSV IAASNSNELF EKILNKKQIQ TKNSIISNMS
     FKGKNPITIF VFSGQGSQYP KMALELYNNE VIFKKSIDLI NSKLSKYYGY SVLEKLRSIG
     DDDTTSIHDP NISQPAVCMI SVSLFELYCH WGVNPSFILG HSLGEISASY CSGMIDLDTF
     CYTVYHRSIA QTKTHGNGRM LSINISDEEF KSMYSQKYPQ IEIACYNSPQ SIVVAGNESI
     LNEISKELKE KEIFTAMLGS LSSFHTSSQQ CTKDSVLKLN IQSNQPKVPI FSTVTTNLFN
     ESNRFNSQYV YDNIINPVRF TQTISNIYKH IESNQLNNDI VFIEIAPHPT LSFYIKQMVP
     SSLNESVSVY SALHKKKNDV EEFQQTISNL YCQNGYNINF KCQFNNKKSN KKIDLPLYQW
     SDETYFAQTQ TLEQHREEGP PIDHLGISNS FISPFNNSYK TLIDINNKPF QYLKGHMVKG
     KYYFPGCGYI DNIIQLYKNQ DIFISFIEFK TPLILIEGIN QCLQTNIQQT GKSEYRAQFH
     FKDQKSNQWT QSSNSNFQLL DHGNDIPSNY NIEEIIKNKC NLSKLTKNEL YTHIKSKTGL
     NYTGVFKGVT ECYIGDNCSL SVVSLESQTN SFLNIPILDT CLHGMLVLIN DQCQIVFDKT
     IGFKYYSSNI PAYFKENKDC FYVYSHLKSK SADSYHGSII VMLSDGSVLY EIQEVVCKSL
     IPIKDSLKIE YPNDELYKVH LQSKDSQIPT PSYFKSIIYE NDSFHSIVNI PEDLFKYIST
     LFYKDIIKRC PEININKINS HSVNEIISSF SKISKHERLF RFVFETIKEN GILNSLEEND
     DAYFEFNELV IKSSRIISKL LFPLENDNDN EDLPQSLFQN GLMDKFYKCN NFKKKNQIIS
     HVIKHSIKEI INNNIIIRIL EFGGGTASLS VEVIGEIVTL LQENPNYQVE IEYTWSDISP
     AFIADAKNKI NKIINDAAIT NGLNVIYLPL TIGESLIETQ SIKPSYYDFV IMSNVLHVVK
     DIKQVVEQMY QLLTPNGQLV FVEPPYKSIL IDSIVGSFDQ WWSFTDTDIR KDRCGMSQQS
     WYQLLKTCNF KDIVMSKECI FGSVIQAQKP PISLLNSQPK HDNIIIYGGG NNSRFFENIK
     LYSNSKSLIQ IETIQEFNQF INKSTITNDS IIYFIKTLET LSLDNFAQIT LEYIEINKKL
     LQINSLCKHV LIVSDSRKTN YLASSVVGAA RYFDEFQQLK LHTLDFDYDS TQNYINSKNN
     KMVQFINILT DSKTNVHKEM IIINNKVYYE IVQKEKNLKL KYNSESFENQ NNLMCSLSPN
     LEYQLQSKQI KLRDNQVEVK TIATGINYKD YLNFSGSNSN GDDNTGLPQF GYEFSGIITR
     VGNNVKDYKV GDNVFGLSNS CTSSHIVTNF KNIQLKPSKI SHIEASSIPI DYLASFISLF
     NVGSLNIEDN ESILIHLGSD GFGLSTFEIL KWKGFKSNLF VTVNSDETKQ YLLDRYGDFI
     SGIYSNTDKS YVTEIKNELI KLGSKKKGVD LILNTLPSDF MDSNFELLTK NARIIDLTSN
     HLNQSEFLKN INFKYNHSYH NFQLSLFQKN KIQKCLNEIS NAIENGELKT IPIKEFTNLN
     IKDAIKYITN GNIEKITVSH DHEIYSDIIY RYLDEKEFSI LKSNYQINSN NLGKNILITG
     QSGIILEILK WIIKYSNINT IENVIILSRS SLKWELELLI NQTKLSNNNI KFHFKSIDVG
     DSEQVDNAIN EILNENQQIT NIDSIYHFAF QQITCKVQEI NMKHLDISHG AKSMGAINLH
     NQSIKRNWKL INFVMASSAI SLIGSTDLCT YACANTLLDS FSKYRVSLGL PSACINFGSI
     ESTGFVSKNE SVSVFLDGGG FHPTPINQVL GLLDLQIQNS GKFTNSMLSN FKPSKFKNNQ
     QISLFLKFDY LMNLKNNSEQ TKKENIGNKN IDELFIEKVS ELFSTDESKI NKNLRLIDYG
     ADSLIIVQLK NWIDKEIGIN LITIQQLQNN TINISIKMIL NSLMKNNQCG REI