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PKS32_DICDI
ID   PKS32_DICDI             Reviewed;        3101 AA.
AC   Q54FP8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable polyketide synthase 32;
DE            Short=dipks32;
DE            EC=2.3.1.-;
GN   Name=pks32; ORFNames=DDB_G0290709;
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).
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 quartet pks29/pks30/pks31/pks32 in
CC       chromosome 5.
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DR   EMBL; AAFI02000167; EAL62089.1; -; Genomic_DNA.
DR   RefSeq; XP_635593.1; XM_630501.1.
DR   SMR; Q54FP8; -.
DR   STRING; 44689.DDB0235258; -.
DR   PaxDb; Q54FP8; -.
DR   EnsemblProtists; EAL62089; EAL62089; DDB_G0290709.
DR   GeneID; 8627790; -.
DR   KEGG; ddi:DDB_G0290709; -.
DR   dictyBase; DDB_G0290709; pks32.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54FP8; -.
DR   OMA; WECVAEF; -.
DR   PhylomeDB; Q54FP8; -.
DR   PRO; PR:Q54FP8; -.
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: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..3101
FT                   /note="Probable polyketide synthase 32"
FT                   /id="PRO_0000371392"
FT   DOMAIN          2550..2627
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          180..233
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          664..697
FT                   /note="Acyl/malonyl transferase"
FT   REGION          1209..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2627..2648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        199
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        674
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2587
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3101 AA;  353160 MW;  E91B966152AE408B CRC64;
     MVQNTDNNTY DQLIRERNDY DDDAGSSGDV AVIGIGLRFP SGSLKESISK PYQLFNELLN
     GLDGIVSTFE RWFDNYYLNG EIVSKFAGLL PLDEWKQFDP IFFAINPSND NVSSIDPQQR
     LLLKCVWEAL EDSGIDPISL RGTNTSTFIG SSTIDYCNLQ KSPSETQNNI FGSSTHSIAN
     RIGFCFDFRG ESLTIDTACS SSSNAINCGY NSIKSNKSNV SIVGGVNFIL DPHISKSFTQ
     LGLLSPTGRC HTFSSDADGY VRSEGVGIVV LKKLKDAIKD SNNIYCVIKG SNSNIDGNFD
     KLNFYSPSKS SQCENIKLAI KSTNGQINES DIDYCETHGT GTPTGDPIEL EGISRVFNTT
     KISSATTITT NNNNKQVLVG SIKSNIGHTE ACSGVASLIK CCLMFKNKLF LQNINFKEPN
     PLINFKEWGL KVVTEPIKFN ENKQTVMLIN NFGVTGSNVC LILSEFKNNH YGNDYHKMKI
     DNKFNEKKRY LIPFSSNSST SLNNYKSSII KHSNSSSTTT SFKEFVHNQI KFKSTSLIQK
     SVIIASDWNE FQDESNQIKL NSSDNLISNI TVEKKKSPLT VMVLCGQGSQ YNKMALSLYD
     NEPIFRESVN RFDKELFKYY GYSVLDKLRS IDDKDLISIH QPILAQPANI MIQVSLYELY
     KHWGVSADII IGHSLGEVSS AYCSGMIDFE TLCYLTYHRS VAQNRTTGTG RMLSVNISSD
     EFINNYQSTT KYESLEIACY NSPTSIVIAG KEDLLNEITN EFKSNDIFCS MLGSLSSFHT
     SSQQMIKDEV CSLNISSKQP SIAVFSTVTT NLFNHQTSPF NANYVFDNII QPVYFTQTIT
     NLYKHIESND MGNEITFIEV SPHPTLQYYL NQMKSTQSSY FNNGKNITIY SPLNKKKNDY
     NEFLKTISLL YVNNNFDINF KSQLINNNNS NNNYENQLNN LPLYQWDDKE YFKLNSSLEK
     IKSEGPSINN LGNNTDSPYP SYQTFIDIKK SPFQWLKGHQ VSDKFYYPGM GYVHNLLSIY
     PNQDITISSL EFKSPLVLTE GNNQCLQTII TPLSKNEFNI KSHYKDQKTN QWILSSLGNF
     SLTKHNSIIS NKLINIQSLK DKCNFTSISK QDLYETIRIK TNLTYKGLFQ GVKQCHIGNN
     CSLAIVSLNE IYNQKEYNHL INNTNMNSFF NAAILDTCLH GSLVAVTQPV VLDRIEGFKY
     YSSNIPSFKN GNNNDDDEES NNNNNNNNNN NNNNNNNIKE LYVFSDIKSR TNSQTYSISV
     KIILPNGTLL VDISNVVCTL VSLPNPESAI ICKPPSNDIY TPYLQSKDSV INKPEQFKHL
     YRVDEFSVNE EDNQFISNEL LLSLFYKHIN NRCPSINLES LTTLEYNQFK QLYYNSSVNE
     NLFKFIFENL KRYSNILNHD NNHSNIKSEN EELYIRTTKI MAKQLFPLKD DDSITDTPQS
     LFESGFLDDF YKNSRVVQPL NNLLSEIIVE TLKPILNEPI VFRILEAGGG TGSLSLLILE
     KICKLLNDNS TTSIINIEFT WSDISASFFA EIKEKFSSFT NHNNLNIIYR VLDLEKPLLD
     QDLKASYYDF VVMSNVMHVV KKLKPTLNEI HNILTPNGQL MFIEPPYKSF YYDSIFGCFS
     QWWPSYDSDI ELRPDRCCMK QEKWINLLNQ CNYRDTIMSG NDNLVFLIQT RKPTINEIIS
     EQSISLDQLN SFNNIILFSN NNNSNDKNRN SCSSSILDLI RLNQELKHKI ININNYNEFQ
     SWITNNQNKD GCNKTLIIFL KSIESKMNTF NFKEITFEYI QINQLILKLE LSNNFKHLLL
     SLNSTTDNYL SSSIVGAARY FVEFPQLDLY ILNYDNVSIE NNQQLSLINY LINPNNNIQK
     EFTINNNKVY YERYCRRSNN IKSIFQSESF ETNKDNLYIQ LNSNLEYQLY SKKDELNSNE
     VEIEIKANGI NYKDYLMYIG MIGSDLDIKY GKEYEIENGI GIDNPNIGND FSGIITRLGS
     NVKKFKVGDQ VCGVGSKTNS SHVIVDYNYI YYKPLNYNHS VSASIPSIYI TSLHSIYSIG
     NLKSNESILI HSAAGGIGIS SLDLLKSKQH QGYIFLTVGS KDKEEYLTKK YGSLITAIYS
     SRNKDYVYEI KNKLIELSVV EQHQQGVDLI LNTLSSEYMD SNFQCLNLSG RIVDLSITHL
     TPNDYMINNH YKFNMGYNNV EVVDFPSKLF KGYLKKIIKM ANSNKLELSV PIIEYSNNQF
     KDAIEYINQR KHIGKIIVNH NQDEFNRVYN NYQNNNNHII MKHSYDISKL NIGKNILLTG
     QTGIVLEILK YLIKYSNHSI ENIIILSKSK LKWELELLIN QSKFKKDNNI KFHFNQIDIE
     DSNKVNQVLN QLELNENITN IDSIIHFAFM NDIGDVQQVD MNRLNNTHGA KTIGAINLHN
     QSINRSWNIK QFIMASSVVS IFGSDQQCCY VSACSVIDSL SKYRHSIGLP SLAINLGAIS
     STGFVSRNNA IETMLKSSIL NLFSPQLVIS SLDLFIQNQH QYPNYCLSDF NFEILPSTLT
     NHFLKKFDYQ INIVKKSNQI KSSSGGNGGD NNEIIRSTIL NKISELLSID ESKINEDLQL
     TQYGMDSLVI VQLKNFIDNQ LGHNIITIQQ LQNNKINQSI EIIKSANNKN NKNNNNNNNN
     KTNKNNNNLV KKEQQSLDEF IKHETKLNES IISRPYSIKN ILNNNNNKSI FLTGSTGFLG
     AYLLTELIKM KNVSKIYCLI RNNSKLTNPI DAIINNLKKH QLINMNKESP NQRSSKILNH
     TGNISNDKLS IIENSENNNK QIREDQLIKI IPMIGDISKD KFGLTEQDYL KLSNECDIII
     NSAADLNLKS NYEESKTVNV DSINQVIKLS VSNNSSQKLI VHFSSIAVFI NHQLKDGETF
     EETNILPNFD TTPVGYIQSK VISEKLLTNA AESRGIPSII IRPPDIFSNP ITGIGHSNDF
     ISLFLKVSKE IGYYPNIHKP IFTTPVTTIA KTTIDLIFNE NSWNQNKSKP ISIYSLNGNS
     IEMKSIYEFL ENKFNCKEID YQEWIKLVSK SNGKSSKRYS AFHIHDNQNL LISNFKINSL
     FKMSNSTKEL LISIGSYNHQ DWEINESIIL NNINNNNKEI K
 
 
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