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PKS27_DICDI
ID   PKS27_DICDI             Reviewed;        2684 AA.
AC   Q54G30;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable polyketide synthase 27;
DE            Short=dipks27;
DE            EC=2.3.1.-;
GN   Name=pks27; ORFNames=DDB_G0290467;
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 pair pks27/pks28 in chromosome 5.
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DR   EMBL; AAFI02000163; EAL62249.1; -; Genomic_DNA.
DR   RefSeq; XP_635742.1; XM_630650.1.
DR   AlphaFoldDB; Q54G30; -.
DR   SMR; Q54G30; -.
DR   STRING; 44689.DDB0235220; -.
DR   PaxDb; Q54G30; -.
DR   EnsemblProtists; EAL62249; EAL62249; DDB_G0290467.
DR   GeneID; 8627660; -.
DR   KEGG; ddi:DDB_G0290467; -.
DR   dictyBase; DDB_G0290467; pks27.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54G30; -.
DR   OMA; WLPDFDF; -.
DR   PhylomeDB; Q54G30; -.
DR   PRO; PR:Q54G30; -.
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; 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; 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..2684
FT                   /note="Probable polyketide synthase 27"
FT                   /id="PRO_0000369418"
FT   DOMAIN          2585..2662
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          164..217
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          650..683
FT                   /note="Acyl/malonyl transferases"
FT   REGION          1202..1221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        660
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2622
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2684 AA;  304919 MW;  B7EDCA3ECD4DB94D CRC64;
     MFGYNSNEED CGDVAIIGIG LRFSSGDLNE SISKPNQLFN SLLDGFNGIV NTSERWSDNY
     YLNGEINSVS AGLLPLDEWK RFDPIFFGIN PSYDNVVTID PQQRLLLKCV WEALEDSGID
     PISLRGTNTS TFIGCSTTDY CSLQKSPFET QNNIFGSSNH SVANRIGYCF DFRGENFTID
     SACSSSLNAI NCGYNSIKSN KSNVSVVGGV NFILDPNISK SFTQLNILSP TGKCHSFSSD
     ADGYVRSEGV GIVILKKLKD AIKDSNNIYC VIKGSSSNID GNYDKLNFYS PSKSSQYENM
     KLAIKSTNGQ INESDIDYCE AHGTGTPTGD PIELEGISRL FSHNNNNNNN NKQVLVGSIK
     SNIGHTEACS GVASLIKCCL MFKNKLFLQN INFKEPNPLI NFKEWALKVV TEPIKFNENK
     TTVMLINNFG VTGSNVCLIL SEFKEKRYNN NEYSSDNACE QIDIDSKVIE KKKFLIPLSS
     NSSTSLDNYK SIIVNNNYDD SNSSTRSFQE FVYNQIKFKS TSLIQKSVII ASDWNEFQDD
     DNQIKLKNSE GLISNITVEK KKSPLTVMVF CGQSSQYNKM ALSLYENEPI FKESVNRFDK
     ELFKYYGYSV LDRLRSVSDK DEISIHLPIL AQPANIMIQI SLYELYKHWG VSADIIVGHS
     LGEMSSSYSS GMIDFETLCY LIYHRSLAQN RTTGTGRMLS VNISYDEFIE KYQSKNNKYE
     TLEIACYNSP TSIVIAGKED LLNEISKEFK SNDIFCAMLG SLSSFHTSSQ FMIKDEVCSL
     VFKSKLPSVP VFSTVTTNLF NDQTPYNANY VWENIYQPVS FTQTISNLYK HIESNDMGNE
     ITFIEVAPHP TLQFYLNQMK SIQSSYFNHG KSVTIYSPLH KKKNDYNEFL KTISLLYVNN
     NFNINFKSQL TNINNNKIKS NSNSNSNKNN NKIIQFNDNN LPLYQWDDNE YFKLNPFHEK
     ITSEGPPIQN LGNSIDSACS TYQTFIDIKK PPFQWLKGHQ VSDKFYYPGM GYVQNLLSIY
     PNQDITISSL EFKSPLVLTE GNNQCLETTV SLLSKNEFNV KSHYKDQKTN QWILSSLGNF
     SLFKHNSINS EKLINIQALK DKCNFTTISK QEFYETIKIK TNLTYKGLFQ GVKECSIGNN
     CSLAVVSLNE INNHTISNHS TIGRSLFNAA TLDSCLHGSL IVVAQPIVLD RIEGFKLYSS
     NIPSSSSSSK DDNDCDSNNN NNSNNFIKEL YVYTEAKAKT NYQSFSASVK IILPNGRLLM
     EISMVVCTSV SLVNPRSSII CKPPSNEIYT PWLQPKDSII NKPQQFKHLY SVDEFIAKEE
     DNQIISTELL LSLFYKHINV RCPTINLESL ITLEYNQFKQ LYYNNNGSVN ENLFKFVFEI
     LKSYSSNNIL NHNNSENNNN ENSNNESLYY FEQLYIKTTK IIAKQLFPLK DDDSFTDTPQ
     SLFKNVYLDE FYKNFRAVQP LNNLLSEIII EALKPILNQP IVFRILEAGG GTGSLSLLIL
     EKICKLLNAN PNSVIDIEFT WSDVSSSFFT EIKEKFSPFT AHKNFNIIHR VLDLEKPLFD
     QDLKPSYYDL VVISNVMHVV KKLKPTLDEI HNILTPNGQL LFIEPPYKSI YYDSIMGCFS
     QWWPSPDSDT ELRPDRSCMN QEKWIKLLNE TNYRDTIISG NDNLIFLIQT RKPSINEIIS
     KQSSDSSLDQ FNSFNKIILF GNNNNNGCSL QNSISSNQEL KSKIININNF NEFQTWITNN
     YDNSDGFGNS KTLIIFLKSI EPINISNFKE ITYEYIQINQ LILKLELTNN FKHLLLSLDS
     TTDNYLSSSI IGAARYFVEY PQLDLYILNY DRISLKILNN SSGSSSSSSS SSSSSISGSS
     GSSYNSSNVS ISSCKQQQLS LINYLINANN NIQKEFTINN NKVYYERYTR HSNKIKCNLQ
     SKSFETNKDN LLIQLDSNLE YQLYSKRVEI NSKEVEIEIK ATGINYKDYL MHIGMVSSDL
     DLKYGKEYEV ENGIGIENPM IGIDFSGIIT RLGSDAERNK FKVGDHVCGV ASKTSGSHVV
     IDYNFIYHQP LNYNHSISAS IPSIYITSLH SIYGVGNLKS NESILIHSAA SGIGISSLDL
     LKCKKHQGHI FLTVGSKDKE DYLIKNYGSF ITAIYSSRNK DYVNEIKNKL IELGEVEQQG
     VDLILNTLSS EFMDSNFQCL NMSGRIVDLS VTHLTPNDYI VNNLFKYNMG YNNVEMLYFN
     GKMVRSYLKK IIKMINSNKL ELSIPIIEYS NNQFKDAIEY VNQGKHIGKI IVNHNQDEFN
     RVYNNYQQNN NNNQIIMKHS YDISKLNMGK NILLTGQTGI ILEIMKYLIR YSNHSIQNMI
     ILSKSKLKWE LELLINQTKF IKDNIIKFHF IQIDIEDSNK VNQVLNQLEL NENITNIDSI
     IHFAFNNDIG DVQDVNMNRL NIAHGAKTIG AINLHNESIN RSWKIKQFII ASSVASVLGS
     DQQCCYISAC SVIDSLSKYR HSLGLPSLAI NLGTIASTGF ISRNNAIETM FKSSFLNLFS
     PQLVISSLDL FIQNQHQYPN YSLIDFNFEV MLTSPNYHLY KFDYEINIFK KSYQINTNFS
     SGSGSDNEFI HSTILNKISE LLSIDESKVN EDLQLTQYGM DSLVIVQLKN FIDNQLGHNL
     ITIHQLQHNK INQSIDIIKF GYLINKNKFK YKNNNINSPS EENF
 
 
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