ID   PKS31_DICDI             Reviewed;        2623 AA.
AC   Q54FQ1;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable polyketide synthase 31;
DE            Short=dipks31;
DE            EC=2.3.1.-;
GN   Name=pks31; ORFNames=DDB_G0290703;
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; EAL62086.1; -; Genomic_DNA.
DR   RefSeq; XP_635590.1; XM_630498.1.
DR   AlphaFoldDB; Q54FQ1; -.
DR   SMR; Q54FQ1; -.
DR   STRING; 44689.DDB0235264; -.
DR   PaxDb; Q54FQ1; -.
DR   PRIDE; Q54FQ1; -.
DR   EnsemblProtists; EAL62086; EAL62086; DDB_G0290703.
DR   GeneID; 8627787; -.
DR   KEGG; ddi:DDB_G0290703; -.
DR   dictyBase; DDB_G0290703; pks31.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54FQ1; -.
DR   OMA; AFYHPDH; -.
DR   PhylomeDB; Q54FQ1; -.
DR   PRO; PR:Q54FQ1; -.
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   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..2623
FT                   /note="Probable polyketide synthase 31"
FT                   /id="PRO_0000371391"
FT   DOMAIN          2524..2601
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..233
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          666..699
FT                   /note="Acyl/malonyl transferase"
FT   REGION          2600..2623
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        676
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2561
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2623 AA;  298926 MW;  E4686CC74E9BF5B3 CRC64;
     MTQNIDNNNN KLIRDRNDDD DVDRNDDGDV AVIGIGLRFP SGNLKESISK PNQLFNELLN
     GLDGIVSTSE RWSDNYYLNG EIVSKFAGLL PLDEWKQFDP IFFAINQTYD NVSSIDPQQR
     LLLKCVWEAL EDSGIDPISL RGTNTSTFIG NSTIDYYNLQ RSPSETQNNI FGSSTHSIAN
     RIGYCFDFRG ENLTIDTACS SSSNAINCGY NSIKTNRSNV SIVGGVNIIL DPHISKSFTQ
     LDMLSPTGKC HTFSSDADGF VRSEGVGIVV LKKLKDAIKD SNNIYCVIKG SSSNIDGNFD
     KLNFYSPSKS SQCENIKLAI KSTNGQINES DIDYCETHGT GTPTGDPIEL EGISRVFNSA
     KIPSTTINNN KQVLVGSIKS NIGHLEACSG VASLIKCCLM FKNKLFLQNI NFKEPNPLIN
     FKEWGLKVVT EPIKFNENKS TVMLVNNFGI TGSNVCLILS ELKKNHHNRY ENEYHKIEID
     SKVNEKKKYL IPLSSNSSTS LNNYKSSIIK LSNSNSSPTT TTSFKELVHN QIKFKSTSLI
     QKSVIIASDW NEFQDENNQI KLENSDNLIS NITVEKKKSP ITVMVLCGQG SQYNKMALSL
     YDNEPIFRES VNRFDKELFK YYGYSVLDKL RSIDDKDLIS IHQPILAQPA NVIIQVSLYE
     LYKHWGVSAD IIIGHSLGEV SSPYCSGMID FQTLCYLIYH RSVAQNRTTG TGRMLSVNIS
     SDEFINNYQS TTKYESLEIA CYNSPTSIVI AGREDLLNEI TNEFKSNNIF CTMLGLLSSF
     HTSSQQMIKD EVCSLNISSK QPSIAVFSTV TTNLFNHQSL PFNADYAFEN IRQPVRFTQT
     ITNLYKHIES NDMGNEITFI EVSPHPTLQY YLNQMKSTQS SYFNNGKNIT IYSPLNKKKN
     DYNEFLKTIS LLYVNNNFDI NFKSQLINDN NNISNTTKLN NLPLYQWDDK EYFKIASFHE
     KIKSEGPSIH SLGNNTDSPY PSYQTFIDIK KSPFQWLKGH QVSDKFYYPG MGYVHNLLSI
     YPNQDITISS LEFKSPLVLT EGNNQCLQTT IAPLSKNEFN IKSHYKDQKT NQWILSSLGN
     FNLTKHNSII SNKLINIQSL KDKCNFTSIS KQDFYETIRI KTNLTYKGLF QGVKQCYIGN
     NCSLSIVSLN EIYNQKEYNH LINNSNMNKF LNTAILDTCL HGSLVAVTQP VVLDRIEGFK
     YYFSNIPSLN ENNNNDDIKE LYVFSDIKPR TNYQTYSISV KIILPNGTLL VDISNVVCAL
     VSLGSNPDST IICKPPLNDI YTPYLQSKDS VVNKPEQFKH LYSVDEFSVN EEDNQFISNE
     LLLSLFYKHI NNRCPSINLE SLTTLEYNQF KQLYYNSLVN ENLFKFIFEN LKRYSNILNH
     DNNQSNIKPK IEKIFIRTTK IMAKQLFPLK DDDSITDTPQ SLFESGFLDD FYKNSRVVQP
     LNNLLSEIIV ETLKPILNEP IVFRILEAGG GTGSLSLLIL EKICKLLNDN STTSIINIEF
     TWSDVSASFF AEIKEKFSSF TNHNNLNIIY RVLDLEKPLL DQDLKASYYD FVVMSNVMHV
     VKKLKPTLNE IHNILTPNGQ LLYIEPPYKS FYFDSIFGCF SQWWPSSDGD IELRPDRCCM
     KQEKWVNLLS QCNYRDTIMS GNDNLLFLIQ TRKPTINEII SEQSISLDQL NSFNNIILFS
     NNKNRNSCSS SILDLIRLNQ ELKHKIININ NYNEFQSWIT NNQNKDNCNK SLIIFLKSIE
     STMNTSNFKE ITFEYIQINQ LILKLELSNN FKHLLLSLNS TTDNYLSSSI IGAARYFVEF
     PQLDLYILNY DNVSIENNQQ LSLINYLINP NNNIQKEFTI NNNKVYYERY CRRSNNIKSK
     FQSESFETNK DNLYIQLNSN IEYQLYSKKD ELNSNEVEIE VKATGINYKD YLMYIGMIGS
     DLDIKYGKEI EYGIGIDNPK IGNDFSGIIT RLGSNVKKFK VGDQVCGFGS KTNSSHVIID
     FNSIYYKPLN CSHSVSASIP SIYITTLHSI YSIGNLKSNE SILIHSAAGG IGISSLDLLK
     SKQHQGYIFL TVGSKDKEEY LINKYGSLIT AIYSSRNKDY VYEIKNKLIE LGVVEQHQQG
     VDLILNTLSS EYMDSNFQCL NLSGRIVDLS ITHLTPNDYM TNNHYKFNMN YGNVDIEDFP
     SKLIKRYLKK IIKMINSNKL ELSVPIIEYS NNQFKDAIEY INQRKHIGKI IVNHNQDEFN
     RVYNNYQSNN NQIIMKHSYD ISKLNIGKNI LLTGQTGIVL EILKYLIKYS NHSIENIIIL
     SKSKLKWELK LLINQSKFKK DNNIKFHFNQ IDIEDSNKVN QVLNQLELNE NITNIDSIIH
     FAFMIDIGDV QQVDMNRLNN AHGAKTIGAI NLHNQSINRS WNIKQFIMAS SVVSIFGSDQ
     QCCYVSACSV IDSLSKYRHS IGLPSLAINL GAISSTGFVS RNNAIETMFK SSIVNLFSPQ
     LVISSLDLFI QNQHQYPNYC LSDFNFEVLT PTLTNQYHSK FDYQINIVKK SNRIKSFSSG
     NSGANNEIIH STILNKISEL LSIDESKINE DLQLSQYGMD SLVIVQLKNF IDNQLGHNII
     TIQQLQNNKI NQSIEIIKSA KNNNKNNNNN NNKNNSNNKN KNN