PKS15_DICDI
ID PKS15_DICDI Reviewed; 3174 AA.
AC Q558W4; Q86B12;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable polyketide synthase 15;
DE Short=dipks15;
DE EC=2.3.1.-;
GN Name=pks15; ORFNames=DDB_G0273007;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 [3]
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.
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DR EMBL; AAFI02000008; EAL71141.2; -; Genomic_DNA.
DR RefSeq; XP_644952.2; XM_639860.2.
DR SMR; Q558W4; -.
DR PaxDb; Q558W4; -.
DR PRIDE; Q558W4; -.
DR EnsemblProtists; EAL71141; EAL71141; DDB_G0273007.
DR GeneID; 8618630; -.
DR KEGG; ddi:DDB_G0273007; -.
DR dictyBase; DDB_G0273007; pks15.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q558W4; -.
DR OMA; QCFQLFT; -.
DR PhylomeDB; Q558W4; -.
DR PRO; PR:Q558W4; -.
DR Proteomes; UP000002195; Chromosome 2.
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; 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; 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; 3.
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 Coiled coil; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..3174
FT /note="Probable polyketide synthase 15"
FT /id="PRO_0000376888"
FT DOMAIN 2653..2730
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 175..231
FT /note="Beta-ketoacyl synthase"
FT REGION 578..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..740
FT /note="Acyl/malonyl transferase"
FT COILED 472..509
FT /evidence="ECO:0000255"
FT COILED 574..604
FT /evidence="ECO:0000255"
FT COILED 1758..1793
FT /evidence="ECO:0000255"
FT ACT_SITE 194
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 717
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2690
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3174 AA; 361566 MW; 1A8910842B322386 CRC64;
MNNNNNNNNN NNNNNTNNII DDNDEIAIVG IGFRLPSGDI SKSNDSPIEL WDNLMNGFDG
IIESRERWSD NFNELGEISN GNAGLLPLDE WKSFDPLFFG INPSEAPSID PQQRLLLKCT
WEALEDARID PMKIRGSNTS VFIGCSTNDY QNQQQNQMNN NKSNIFGLTN HSISNRISYC
FDFRNESITI DTACSSSLNA IKMGYQSIKF SKQNNCNLSI VGGVNLLLDT NVSKSFTHLN
MLSKSTNGTA RCMTFDESAD GYVRGEGVGI VVLKSLKQAL SDGNTIYCII NGASSNVDGG
GLKDKQNFFS PSSISQCENI KMAIQSTNGK IKFNNIDYIE AHGTGTPTGD PIELEAISNS
FKQLNDIAIG SGSCSGSNNN TTQQPLLIGS IKSSIGHLEA ASGVASLIKC CLMFKNGYFV
PNINFNKPNP MIKFNEWNLK VVTEPIQFNT NKQITMLINS FGITGSNCCL ILSQFKNNEN
QQQQQQQQQQ QQQQQQQQQQ QRGQQQYDNS QPKKYLIPFS ANSTLSLKKY QSIIESEEFQ
LKINFNEFVK NQIFNKSLSL YQRLVIFSVS NWDEFNKQKQ SQKEKEKEKE REGEEKEQLN
RVQTLNSKSS TMSMVHSKNP IVVFVFAGQG SQYSRMAMEL YNSEPIFKQS INMFDNKLFK
YYGYSVFEKF ISITDHDDDI SIQHPTIAQP IMCMLAISLF EFYKHWGIEA SFIVGHSLGE
IPAAYCSGMI TLDTLCYLIY HRSLAQIQTH CNGGRMLSVN ISSEDYLSSN YSTKYPDIEI
ACYNSPNSIV LGGKEQQLNQ ISNELKDKGI FSKMLASLSS FHTSNQKIVK DDISKLNIDY
ELPKIPIFST VTTNLYYNNF NDSNNNSNNN NNNVETTTTP FNSEYIYNNI VEPVKFSQTI
SNLYKHIEIN KLGTDIVFIE LAPHPTLQFY LKQMIPVSTN YFSGKISIYS PLHKKKNDTM
EIQKTIAKLY CENRYNINFK SQFDCGSINN HNHTVIPPLQ QPQPQPLPNY QWDDEKYWKE
DLIQQKHRIE GPPIDILGLS NYDNSSNVKS YQTFIDIKKE PFKYLKGHIV NGKYYFPGCG
YIDNLLKLYP SQDLTISSME FKSPLILIDG INQCLQTNVF QTGKTEFKLY YHFKDNKSNE
WVQSCIANFQ LLNNNNSNNN NSNNNNNNKK LNLQEIISKK CNKTKISRID LYQHIKSKTG
LTYNDEFQGV IQCFLGDSCS LSEVTVNSST SKSFFKTQLL DSCLHGMIAL IQENCQLVFH
KIEGLKYYSS NLQVYETNDI NSSNNSIFVY SKFKSRLGNS YLASIIIMLK DGTILIEIER
VICKSLKIVK NPLEIEYPID LVYSRYLQPR DSPIGAPSSF KSLYESDQFK SKDIYSSNIS
IYQNFISSSL FLNINKRNSN ITIKEIENQS IDQLFLNFKS IFINKNLENS IQYERLFKSV
FKTIKMFGYK NNNNNNFKEL KKQMENNNNY KILKRSTRVI SKQLFPFENE NDSNLDSPQI
LFEDGLLDKF YSDTEFVAKN HQLLAEIIKE SIKPLVLKKE KITIRILEFG GGVSSLSMVV
LNKITQLLEE SNNVFNQIDI EYTWSDISTS FIPDAKLKLS KIINNNNNNN NNENNNDLDL
DGGKFGIKII YRSLDLEEPL IEKQNLKYSY YDYVIMSNVL HVVKDIRFSI DQIYKVLVPN
GQLLFIEPPF NSIILDNVFG VFNQWWSFQD TDIRKDSCCM NQQSWFDLLT NHNFKYIIMS
KELESVSFLI HCKKPSILEI NINNNNNNNN NNNNNNNNNN NNNNNNNNYE DNVIIFCNEI
DKDNKNNNNH FIKMLESIYS FKIIIKISSI KEFIELEESN IITNKSIIYF IKPIEQLNFE
NFKLVTFEFI EINKRLLSSN NLKCKHVLIT TNVNNGKNYL SASVIGAAKY FEEFSEQLQL
FYIDFDQQSI ENLNLISKID SLIDETINTQ KEFIIMNNEI YYERYKKESI KNLINTFKSN
SFEYGIGVSN DSFSNVYLKL TSNLEYKLKS RKEIIKSNKV EVNVLSLGVN YKDYLVYCGL
VPPEICNRKG DINNPEIGID FSGIITRVGK DCGEDQFKVG DEVYGIAFDS SSSHIIIDKD
YIVKKPTNLS HSEAASIPAV YLTSLYSIFN IGNFNIQDNE SILIHSGTGG VGLSALNILK
WKGHKSHLFV TVGSKEKEQY LIDTYGDFIT GIYSTRNKDY VKQIKLKLKQ LGSNKKGVDL
ILNTLSSDYL DSNFKCLECG GRIVDLSITH LNPNEYIDFS KFKYNYGYHN VELLFINKRK
LQILFLQISN AIENNQLNLI PINEYSNLKI KEAIEFINER KHIGKIIVNN NINLINKLIE
NNNFNSSSSS GSSSGSGSID VKEPILKSNY KINNDNLGST ILVTGQTGIV LEILKWIVKF
SDCVKDIIIF SKSPMKWELE LLVNNNSNIR FHFKSIDICN ESLVNESIDQ ILKDNPLINN
VDSIFHFAFQ QVSRKVNKID MESLDISHGA KTFGAINLHN QSIKRNWKLK QFVMASSIAS
IIGSSKQCSY VCANNVLDSL SRFRKSIGLP SICTNYGSLG DAGFVSRFES VGEMLVGQGL
NPISTNLILG SLDLQIQNQH LSTNLLICNF NFPAFKVNAQ IPKQKFDFII NSIDGGGGGS
NSSSGSGGGG KVVDSLNIKD IFINKISEFL SIESSKINQD LRLLDYGADS LLTVQLKNWI
DKEISPNIIT IQQIQNNTIS LVIKIIITAI DNKKIKDSNQ QSNNNENIKT GSFIGGKSKN
NNVKNLKFWK KQIKLKVIGN EFSSSTSSYV NITKNGGTSK NNKRILFPFS SGGYLSTYLL
FNLVKDSNCS IVYCLNTSID LIIQSLKYHQ LYFNLNQNEI SKINIISVSS EKDYNQLFIK
NNDINLIIIV SSDSFQDSIL FEQEFNETEL NLVKELIKSL IINGYCNNND NNNNNNNNKI
SIINISSIYI YLGISNEFIN ENEYNSIEIP NFESIEKLPL SSGKIQSSLL IEHFLKDCSI
KFNIPSTMIR IPPIFSNIET GLGNENELLQ LFLQSCHSIG FYPNVSTSYP TIPINHLSNL
IINQINNQNY YEHDNEKGKL LFNTINLNNN NSNNNNINSQ QINQILKCEF NCKQIEFNDW
IQILTDSNNS SCVYKYLQLH NIITKYSNSN TDTIQENNLE IINQMIINHL KQKK
