PKS18_DICDI
ID PKS18_DICDI Reviewed; 2999 AA.
AC Q54TW0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable polyketide synthase 18;
DE Short=dipks18;
DE EC=2.3.1.-;
GN Name=pks18; ORFNames=DDB_G0281475;
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).
RN [3]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by P.aeruginosa, PAO1 strain and PA14 strain
CC infection. {ECO:0000269|PubMed:18590548}.
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 3.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000041; EAL66719.1; -; Genomic_DNA.
DR RefSeq; XP_640701.1; XM_635609.1.
DR SMR; Q54TW0; -.
DR STRING; 44689.DDB0235183; -.
DR PaxDb; Q54TW0; -.
DR EnsemblProtists; EAL66719; EAL66719; DDB_G0281475.
DR GeneID; 8623087; -.
DR KEGG; ddi:DDB_G0281475; -.
DR dictyBase; DDB_G0281475; pks18.
DR eggNOG; KOG1202; Eukaryota.
DR eggNOG; KOG1221; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q54TW0; -.
DR OMA; WECLENS; -.
DR PhylomeDB; Q54TW0; -.
DR PRO; PR:Q54TW0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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 2: Evidence at transcript level;
KW Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..2999
FT /note="Probable polyketide synthase 18"
FT /id="PRO_0000371383"
FT TRANSMEM 1448..1468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2620..2640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2476..2553
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 168..221
FT /note="Beta-ketoacyl synthase"
FT REGION 651..684
FT /note="Acyl/malonyl transferase"
FT REGION 1066..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2556..2575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 661
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2513
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2999 AA; 339544 MW; FFD29B5F1927E5F5 CRC64;
MGFKVNKNLN ETNDNSDNDV AIIGIGFRLP SGNLNKSNDS PIILWDNLMK GFDGMVETSE
RWSDNFNQLG EISNKSGGLL PLDEWKSFDP LFFGINPSEA QTIDPQQRIL LKCTWEAIED
SNIDPIKIRG SKTSVYMGGT SVEYKELNKN SNEINPNIFG STFNTIANRI SYCFDLSGES
MTLDTACSSS LNAIILGYQS IKSGTSNLSI VGGVNLILDS NLSKSYSYLN MLSKKEGKCM
SFDSRADGFV RSEGAGVFIL KSLKQSIIDG NNIYCVIKGA SSNIDGNGLN DKQNFYSPSS
SSQAENINRA LSSTKGSVKI DDIVYVEAHG TGTPTGDPIE LEAISRVFKT NNNDNNNQQH
QNPILIGSFK SSVGHLESAS GSASLVKCCL MFKNQYLTPN VNFKTPNPSI KFDEWNLKVV
TEPIQFKDVK KSNNFSMILN NFGITGSNCC LILSQYNGNH NDEQENQQQQ QQQGKQYLIP
FSANSIQSLK QYESLINENQ FKESNDFKEF VKHQIYSKSI SLYQRSVSIA SNWNDFNEGM
KSTNNNNNKT QTSNSKSSNI SIIPKNPITV MVFAGQGSQY STMAMELYNN EPIFKESMDR
LDNRLLRYYG YSVLEKFRSS CDSDSIHYPT IAQPSMCMLT ISLFELYKHW GIETSFIIGH
SLGEIPAAYC SGMISLDTLC FLIYHRSVAQ THTHRNGRML SINISPEEYN SNYSLKYPKV
EIACYNSPTS IVLGGEETIL NQISNDLKEK GIFSAMLGSL SSFHTSSQRI IKDQVIDLNI
ECKLAKIPSF STVTTNLFNE TTLFNSEYIF NNMALPVKFS QSISNLFKHI EINNLGSDIV
FIELAPHPTL QFYLKQMASS YEKVNSNLKI STYSPLHKKK NDIEEIQKTI SQLYCNNGYS
INFKSQFNND FKINKINSIL PNYQWEDVIH WREDLIHQKH NTQGPPIDQL GLSLIESSPN
LKSYQTFIDI SRKPFQYLKG HFVNGKYYFP GCGYIDNLLK IYGSQDFTIA SMEFKSPLIF
TEGVSQCLQT NIFQTGKSEF RVNYHFKDTK SNEWIQSSVA HFQLFNNNNN NNNNNNNNNN
NNNNNNNDSD DGNSTNKKYN IEDIINNKCN FTKLSNNELY ENIKSKTGIY YTGEFKTVSN
LYVGENCSLA EIPITIKSYE SSFFSPSILD TCLHGTIGLI DEKSQIVFER VEGFEYHSSN
IPSQNELSSL KHTKLYSLTE SFKRVGDSYS SSITVMLEDG RVLIEFKKVV CKSLTNVIDS
LIIQSPLNEL YSTCMQTIDS PIQPSLSSSS LIQLLGNTNE KVKINYSQFI SNQLYYNIIK
RCPQLNIETI KSKNIEQLKE SYNSLNTKYS KLFKSVFETI QSIGINNEDN SEFNETNIQH
YKILLKSTRI IAKLLFPLKD DDLSKDTGQS LFENGILDEF NSNYFNNNNQ VISNIIKESL
LPILNEKMVF RIFGFGGFGS SLSSVVLNKI NELLQEFPNS EIDIEFTHAD ISSSSSSFGS
STPNFKPNFP QINEKVHIIY KSLDLEKQLS SEQMIKPSYY DFVIMSNVLH FTKDVKSVLD
QIHQILKPNG QIILVEPINK SILLDNIFGI FDQWWSFTDL NIRRNDCYIS KDTWNSLLLD
CNFDNSKVLI STKEISNFYI IQTQKPSISN LNTNSTTNGD TVIIYGDELK FISSDSNKEI
KISNIQQFNE LIEKSIITDE SIIYFTKSTN QLTVDNFKLV TLEYIQINQK LLSNNLKCKH
VLITLNSDNM NYLSASLIGA TRYFEEFPQL NLFNLDFDQN SINNNELEKT IKLLLDSNQF
IQKEFFIKNS KVYYERYKRE LNLNNFFKES QSFSNEKNQL YAKLSPNLEY ILKSKKVIKD
DEIEVEVKAT GINYKDYLIY CGLVSAESIN RYGDVNNPEF GIEYSGIISR IGNNITNFEI
GDQVYGMGLD TISTHVIVNP NYCYHKPTNI SFQEAASIPC VYLTSLCSIF NIGCLSVSGN
ESILIHSGTG GVGLSALNIL KWKGHKSHVF VTVGSKEKEK YLLDTYGDFI TGIYSTRNKN
YVEQIKLKLK QLGSNKNGVD LILNTLSSDY MESNFKCLNT SGRIVDLSVT HLNHNEYINN
NNFKFNFGYH NFELTFINKF LIQKSLKKIK IGIESGELKL IPITAYSNSN AKEAIEFINQ
RKHIGKIVLN NDNDILDSLF NNLSNERNSK FTTLKPNYQI NKDHLGSNII VTGQSGIILE
ILKWIVKFSE NVKNIIILSK SSMKWGLELL IKKNKHINFN FKSIDIGDSN QVDKSIDEIL
NENSITNIDS IFHFAFEHTI CDVNDIEINH LTKSHGAKTM GAINLHNQSI KRNWKLKQFI
LSSSVTSMIG STDQCTYVCS NRLLDSLSKY RNSIGLPSIC TNYGSVQSAG IVSRNKSIEK
LLDAQGLDPL SINMILGSLD SQIQNVNKST NLMVSPFNFN NFFETFKNHS MIHKFDFITN
LLENNKSKNS NNGNTEGESN IDTLFLNKVS ELLSMELPKI NQDLKLVEYG SDSLLIVQLK
NWIDKEIFPN LITIQQLQTN TISSSIKIIT NQFNSKSTDG RKKQKQNGIN VSSNKSSLPT
LEFWKNETKL DEEEFNFILD SSTKSKINHK DQLKDNEKRI LLTGSTGFLG AYLLWHLIQM
DNCKIVYCLL RNKKLFNNPL NDIIDNLKHH QLYDKQLNES HLSKIVAVVG DLSKIKFGLS
DDNYSLLSND TNLLLNCGAD INLSSNYEES KQVNVVGTKE MIKISLIGNI KPKPIITISS
FSVFYNQKLN QEFDESIVTP KLETINDLPA GYIQSKVISE IILTEASSRF NIPSAIIRAP
SIFSNPETGI GHSADIIQLM LQSCFKLGYY PSGNGVDFDL LCSPITWVAD NTIKIIFNDN
IINNKEPQQL TSPLKPNIYS VYGKVLDLFE ILQVLKSDEG GNCKEIEINQ WKQMVMDSKE
KACIKLRTFH TLQFDGRNIL NKGHGISNKQ KSYLQSIGSF GNGGEITNQM IFKNVQSNN