ID   PKS30_DICDI             Reviewed;        3075 AA.
AC   Q54FQ2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable polyketide synthase 30;
DE            Short=dipks30;
DE            EC=2.3.1.-;
GN   Name=pks30; ORFNames=DDB_G0290701;
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).
RN   [3]
RP   FUNCTION.
RX   PubMed=18164290; DOI=10.1016/j.yexcr.2007.12.002;
RA   Nagasaki A., Uyeda T.Q.P.;
RT   "Screening of genes involved in cell migration in Dictyostelium.";
RL   Exp. Cell Res. 314:1136-1146(2008).
CC   -!- FUNCTION: Probable polyketide synthase (By similarity). May be involved
CC       in the process of cell migration. {ECO:0000250,
CC       ECO:0000269|PubMed:18164290}.
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 quartet pks29/pks30/pks31/pks32 in
CC       chromosome 5.
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DR   EMBL; AAFI02000167; EAL62085.1; -; Genomic_DNA.
DR   RefSeq; XP_635589.1; XM_630497.1.
DR   SMR; Q54FQ2; -.
DR   STRING; 44689.DDB0235263; -.
DR   PaxDb; Q54FQ2; -.
DR   EnsemblProtists; EAL62085; EAL62085; DDB_G0290701.
DR   GeneID; 8627786; -.
DR   KEGG; ddi:DDB_G0290701; -.
DR   dictyBase; DDB_G0290701; pks30.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54FQ2; -.
DR   OMA; WYLHEAT; -.
DR   PhylomeDB; Q54FQ2; -.
DR   PRO; PR:Q54FQ2; -.
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:0048870; P:cell motility; IGI:dictyBase.
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; IPR013154; ADH_N.
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; 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; IPR010080; Thioester_reductase-like_dom.
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; 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   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..3075
FT                   /note="Probable polyketide synthase 30"
FT                   /id="PRO_0000371390"
FT   DOMAIN          2533..2610
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          179..232
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          663..696
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        198
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        673
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2570
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3075 AA;  349549 MW;  034D04EA30186AD2 CRC64;
     MVQNTDNNTY NQLIRDINDY DDAGSSGDVA VIGIGLRFPS GSLKESISKP NQLFNELLNG
     LDGIVTTSER WSDNYFLNGE IASKFAGLLP LDEWKQFDPI FFAINPSNDN VSSIDPQQRF
     LLKCVWEALE DSGIDPISLR GTNTSTFIGS STIDYNNLQK SSFETQNNIF GSSTHSVANR
     IGYCFDFRGE NLTIDTACSS SSNAINCGYN SIKSNKSNVS IVGGVNFILD PHISKSFTQL
     GLLSPTGRCH TFSSDADGYV RSEGVGIVVL KKLKDAIKDS NNIYCVIKGS SSNIDGNFDK
     LNFYSPSKSS QYENIKLAIK STNGQINESD IDYCETHGTG TPTGDPIELE GISRVFNKAP
     ATTNNNHKQV LIGSIKSNIG HTEACSGVAS LIKCCLMFKN KLFLQNINFK EPNPLINFKE
     WGLKVVTEPI KFNENKSTVM LINNFGVTGS NVCLILSEFK NNLSRYGNGN GYHKMEIDNN
     LNEKKKYLIP LSSNSSTSLN NYKSSIIKHS NSNSSPTTTS FKEFVYNQIK FKSTSLIQKS
     VIIASDWNEF QDESNQIKLN NSDNLISNIT VEKKKSPITV MVLCGQGSQY NKMALSLYDN
     EPIFRESVNR FDKELFKYYG YSVLDKLRSI DDKDLISIHQ PILAQPANVI IQVSLYELYK
     HWGVSADIII GHSLGEVSSP YCSGMIDFQT LCYLTYHRSV AQNRTTGTGR MLSVNISSDE
     FINKYQSTTK YKSLEIACYN SPTSIVIAGN EDLLNEITNE FKSNDIFCSM LGSLSSFHTS
     SQQMIKDEVC SLNISSKQPS IAVFSTVTTN LFNHQTSPFN ANYVFDNIIQ PVYFTQTITN
     LYKHIESNDM GNEITFIEVS PHPTLQYYLN QMKSTQSSYF NNGKNITIYS PLNKKKNDYN
     EFLKTISLLY VNNNFDINFK SQLINDNNNI SNTTKLNNLP LYQWDDKEYF KLNSSLEKIK
     SEGPSINNLG NNTDSPYLSY QTFIDIKKSP FQWLKGHQVS DKFYYPGMGY VHNLLSIYPN
     QDITISSLEF KSPLVLTEGN NQCLQTIIAP LSKNEFNIKS HYKDQKTNQW ILSSLGNFSL
     TKHNSITSNK LINIQSLKDK CNFTSMSKQD FYETIRIKTN LTYKGLFQGV KQCYIGNNCS
     LAIVSLNEIY NQKEYNHLIN NNNMNTFFNA AILDTCLHGS LVAVTQPVVL DKIEAFKFYS
     SNIPLLNKNN NNNNSDDDSI KELYVFSDIK PRTNSQTYSV SVKVILPNGT LLVDISNVVC
     ALVSLGSNPD STIICKPPSN DIYTPYLQLK DSIINKPEQF KHLYSVDEFS VKEEDNQFIS
     NELLLSLFYK HINNRSPSIN LESLTTLEYN QFKQLYYNSL ANENLFKFIF ENLKRYSNIL
     NHDNNHSNIK SKHEELYIRT TKIMAKQLFP LKDDDSITDT PQSLFESGFL DDFYKNSRVV
     QPLNNLLSEI IVETLKPILN EPIVFRILEA GGGTGSLSLL ILEKICKLLN DNSTTSIINI
     EFTWSDVSAS FFAEIKEKFS SFTNHNNLNI IYRVLDLEKP LLDQDLKASY YDFIVMSNVM
     HVVKKLKPTL NEIHNILTPN GQLLYIEPPY KSFYYDSIFG CFSQWWPSSD SDIELRPDRC
     CMKQEKWINL LNQCNYRDTI MSGNDNLLFL IQTRKPTINE IISEQSISLD QLNSFNNIIL
     FCNNNNSNDK NRNSCSSSIL DLIRSNQELK HKIININNYN EFQSWITNNQ NKDDCNKTLI
     IFLKSIESTM NTFNFKEITF EYIQINQLIL KLELSNNFKH LLLSLNSSTD NYLSSSIIGA
     ARYFVEFPQL DLYILNYDNV SIENNQQLSL INYLINPNNN IQKEFTINNN KVYYERYCRR
     SNNIKSIFQS ESFETNKDNL YIQLNSNLEY QLYSKKAELN SNEVEIEVKA NGINYKDYLM
     YIGMIGTDLD IKYGKEYEIE NGIGIDNPNI GNDFSGIITR LGSNVKKFKV GDQVCGIGSK
     TNSSHVIIDF NFIYYKPLNY NHSVSASIPS IYITSLHSIY SIGNLKSNES ILIHSAAGGV
     GISSLDLLKS KQHQGYIFLT VGSKDKEEYL TKKYGSLITA IYSSRNKDYV YEIKNKLIEL
     GVVEQNQQGV DIILNTLSSE YMDSNFQCLN MSGCIVDLSI THLTPNDYMT NNHYKFNMGY
     NNVEVVDFPS KLIKSYLKKI IKMINSNELE LSVPIIEYSN NQFKDAIEYI NQRKHIGKII
     VNHNQDEFNR VYNNYQSNNN QIIMKHSYDI SKLNIGKNIL LTGQTGIVLE ILKYLVKYSN
     HSIENIIILS KSKLKWELEL LINQSKFKKD NNIKFHFNQI DIEDSNKVNQ VLNQLELNEN
     ITNIDSIIHF AFMNDIGDVQ QVDMNRLNNA HGAKTIGAIN LHNQSINRSW NIKQFIMASS
     IVSIFGSDQQ CCYVSACSVI DSLSKYRHSI GLPSLAINLG AISSTGFISR NNAIETMFKS
     SILKLFSPQL VISSLDLFIQ NQHQYPNYCL SDFNFEVLPS TLTNHFLTKF DYQINISKKL
     SQIKSSSSGN GGDNNEIIRS TILNKICELL SIDESKINED LQLTQYGMDS LVIVQLKNFI
     DNQIGHNLIT IQQLQNNKIN QSIEIIKSAH INNNKNKNNN NNNNLVKKEQ QSLDEFIKNE
     IKLNESIISR PYSIKNILNN NNNKSIFLTG STGFLGAYLL TELIKMDNIS KIYCLIRNNS
     KLTNPIDVII NNLKKHQLID MNKESPNQRL TKIINRTGNM SNDKLNSNIE NSENNNKQIS
     EDQLIKIIPM IGDVSKDKFG LTEQDYLKLS NECDIIINSA ADLNLKSNYE ESKTVNVDSI
     NQVIKLSVSN NSSQKLIVHF SSIAVFINHQ LKDGETFEET NILPNFYTTP IGYIQCKVIS
     EKLLTNAAES RGIPSIIIRP PDIFSNPITG IGHSNDFVSL LLKVSKEIGY YPNIHKPIFT
     TPITTIAKTT IDLIFNENSW NQNKSKPISI YSLNGNSIEM KSIYEFLENK FNCKEIDYQE
     WIKLVSKSNG KSSKRYSAFH IHDNQNLLIS TFKINSLFKM SNSTKELLIS IGSYNHQDWE
     INESIILNNI NSNSN