ID   PKS26_DICDI             Reviewed;        2531 AA.
AC   Q54IX3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable polyketide synthase 26;
DE            Short=dipks26;
DE            EC=2.3.1.-;
GN   Name=pks26; ORFNames=DDB_G0288457;
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 localized in chromosome 5.
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DR   EMBL; AAFI02000111; EAL63254.1; -; Genomic_DNA.
DR   RefSeq; XP_636757.1; XM_631665.1.
DR   AlphaFoldDB; Q54IX3; -.
DR   SMR; Q54IX3; -.
DR   PaxDb; Q54IX3; -.
DR   PRIDE; Q54IX3; -.
DR   EnsemblProtists; EAL63254; EAL63254; DDB_G0288457.
DR   GeneID; 8626635; -.
DR   KEGG; ddi:DDB_G0288457; -.
DR   dictyBase; DDB_G0288457; pks26.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54IX3; -.
DR   PhylomeDB; Q54IX3; -.
DR   PRO; PR:Q54IX3; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; 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; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2531
FT                   /note="Probable polyketide synthase 26"
FT                   /id="PRO_0000371388"
FT   DOMAIN          2431..2509
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          155..208
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          620..653
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        174
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        630
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2468
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2531 AA;  287781 MW;  017B776B3C5E8124 CRC64;
     METNNNKNIQ EDIAIIGFRI PGCQDNTPSE LWNNLMNKFS GVGKTTERWS DNYHLSGDIN
     NGNSGLLPLK EWKKFDPAFF GINPTMVSTI DPQQRILLKC TWEALEDAGI DPIKLRGSNT
     SIFIGCSTGD YLDMVKSNNE IQTNLFGSVN HSLSNRISYC FDFHGASMTI DSACSSSLNT
     VLLGCQSINQ GKSNLCIAGG VNFILDTTIP TAFSFLNILS KNGKCMTYDE GADGFVRGEG
     AGLVVLKSLK DAIKDGNNIY CIIKGGNTNV DGNGNADKAN FFQPSKQSQS DNIKLALESI
     KKKSMLDIDI DYVETHGTGT PTGDPIEVEG ISKVFKENHS PENPLLIGSL KSNIGHMEAA
     SGVTSLIKCC LMFKNKSFAP NVNFQKINPK IKLDEWNIKV VTEAIPFKKN KITSMVVNSF
     GVTGSNCCLV LTESINNNNN SNVDKITKNE KEYLIPFSAN SNQSLKNYIE EVSKIDESLQ
     FEDFVYKQLS NKSTSLFQRF VVTSKDWKEL KYKLSQPLPL KEISSSISVK KPNPITVFVF
     CGQGSQFNKM GLELYNNDKN FRNYIDRFDK KLLEYYGYSV ISKLRSIDDN DLITIHDPII
     AQPATAILQI SLFELYKHWG INPSFIVGHS LGELPMAFCS GMIDFDTVCY LLYHRSLAQS
     KTNGCGKMLS CNISSEEFVK NYSPRYPFLE IACYNSPNSI VVAGKESILL ELSKEFKNSG
     IFCAMLGSLS SFHTSSQLEV KDHIYSLKFE SKEPVIPTFS TVTTHLFNSN KLYDNDYIFQ
     NIMKPVLFNE TISNLYKHVE NNQLGSEMIF IELAPHQTLS FYLKQLIPKD SNYFSNSNSI
     TILSPLHKKK NDYLEIQQTI STCYCKGYDV NFKSQILIES KTNISNKSLP LYQWDDKEFW
     KDLEKQKRIL QGPPMDTLGF SNEKSPILKS FETKIDIKKK PFQYLKGHIV KGKIYFPGVG
     YIENLLKMYP SQDIDIDSME FEAPLILIEG IVTCLQSNVY KIGKNEFKVQ FHFQDQKTKQ
     WIQSSFANYH LSHRDDFDPT TNKLNIQNLI SNNCNLTKLS KNQFYNFIKA KAGLSYNGEF
     QGVEKCYLGD NCSLVEIPFD TSNQDVETNI NMIPILDSCL HGVHILYVEQ CQMVLEKIEG
     LKYYSSTLIL SKQKEQQKLY VFTRIENKDL INNSISASII VMISDGTVFF EIESVSLKSL
     IPLKDPISIE NPTDELFSSY LQSIDSLISE PSSYKSIYKR NEFISSGMSD LSRSDYQQFI
     STLLYTNLIK RNQSIESDLR NQIEFEEIKA KYCKNSKFER LFTFVIETIK QYDGINGNLN
     SWNEGNIDIY KILIKSTRII SKLLFPLQGE DTTIDTPQSL FENNLLDDFY NINGNTVIQN
     QLVGEIITQS IKPLINEKMV FRILEFGGGV GSLSIVTLNK INQLLEQHPN FQIDIEYTWT
     DISPSFIPDA KKLLSNIKGV TIIYRSLDLE ESLIEKQLLK PSYYDFVIMS NVLHVIKEIK
     FGIDEIYKVL SPNGQLLFIE TPYRMLICDS IFGVFDQWWG FTDTGIRVDR CCMKQKTWFK
     LLSESNYQDI IMSDDIKDCC FVIQAKKPSI SSLEYKLKID SQENDKIIVF GENDTFMKYL
     ENKSTKQIIK IKTCQQFSDL ITSNSKEINN QSIIYFIKTL NQLLIENFKE ITLEYIQINQ
     LLLSSGLSCK HILLLNQSTS ENYLGSSISG AARYFDEFPP LKLYSFDFDK YSLNNESINI
     IDDIIEPIIK SMNNSNIRKE LLVRNNKIFF ERYKQEKRIK ENYKSTSFEN DKSLFVHLNA
     NLEYELKSKQ VKLKQNEIEV NVKATGINYK DYLVYTAMTP SELINHKGES NPEFGHDFSG
     IITRIGDDDG DNDNEFKVGD QVYGIWFNTT ASHIIVDKEF LCHKPSKLSH TIASSIPVVY
     ITSLYSLYNI GNIQNDESIL IHSASGGIGL SALNILKWKN HKSHIFVTVG SKEKEKYIHD
     TYGDFITGIY SSRNKDYLKL IKRKLTELGS NKKGVDIILN TLSSSEHMVS NFKCLNHRGR
     IIDLSITHLN HNEYTCNNNF KYNYGYHNVE VLFVKGDIIS KLLKNITSAI ENGSLSTGIP
     IIEFNDSDCF NAIEFINKRQ HIGKIVVNHN KENLIQELIK KTNLPIIKSN YQINSDHLGK
     NILVTGQSGI ILEILKWIVK YSTNVENIII LSRSSLKWEL ELLVNKNKNK LNFIYKSVDV
     GNSLEIEKVI DEILMENPQI NNVDSIFHYA FTQISCKEHE IDQVHLNVSH QAKTMGAINL
     HNQSIKRNWK LINFIMASSA AGLIGSTDQC SYVCSSNVLD TFSKYRKHVL GLPSICINYG
     LIESTGFVSR NQSVAVMLDG QGIRPMQTNQ ILGSLDLFIQ NPSKSTNIIL TSFNFNEFAT
     GNLQQSNVHK FDFQFNCCLS QKSKLMANNQ ASENPVKDLL INNICELLSI DESKLNIDIR
     LIDYGSDSLT IVQIKNLIDK NLLIPNLISI QMLQNNSISD NIKILTDSYN KKKQNEQNEL
     KNIKVGSFTK K