ID   PKS6_DICDI              Reviewed;        2924 AA.
AC   B0G0Z9; Q86AE8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable polyketide synthase 6;
DE            Short=dipks6;
DE            EC=2.3.1.-;
GN   Name=pks6; ORFNames=DDB_G0271524;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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 quintuplet pks5/pks6/pks7/pks8/pks9
CC       in chromosome 2.
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DR   EMBL; AAFI02000006; EDR41104.1; -; Genomic_DNA.
DR   RefSeq; XP_001732962.1; XM_001732910.1.
DR   SMR; B0G0Z9; -.
DR   STRING; 44689.DDB0235162; -.
DR   PaxDb; B0G0Z9; -.
DR   EnsemblProtists; EDR41104; EDR41104; DDB_G0271524.
DR   GeneID; 8618015; -.
DR   KEGG; ddi:DDB_G0271524; -.
DR   dictyBase; DDB_G0271524; pks6.
DR   eggNOG; KOG1202; Eukaryota.
DR   eggNOG; KOG1221; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; B0G0Z9; -.
DR   PhylomeDB; B0G0Z9; -.
DR   PRO; PR:B0G0Z9; -.
DR   Proteomes; UP000002195; Chromosome 2.
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; 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; 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   3: Inferred from homology;
KW   Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..2924
FT                   /note="Probable polyketide synthase 6"
FT                   /id="PRO_0000376881"
FT   TRANSMEM        2551..2571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2431..2508
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          162..215
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          635..668
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        181
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        645
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2468
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2924 AA;  332524 MW;  331890E0F82FD8AD CRC64;
     MNNLKNIDLI EKGVAIVGIG FRIPSGNNEN SICSPDDLFN NLKNGFDGVS STSERWSDNY
     HKLGEISSPN AGLLPLNEWK SFDPLFFGIN PSEASLIDPQ QRLLLKCTWE ALEDASIDPI
     SIRGTNTSVF IGASNIDYQH TNKHQDSVLK NAIAQSTCAI SNRISYCFDF NGPSLSIDTA
     CSSSLNAVSQ GYHSILNGTS DISIVGGVNL ILDVEMTKAY SYLSMLSKTH GKCKAFDESG
     DGFTRGECVG VVVLKNLQDA IKDGNRIYCV INGSSSNVDG NGNMDKVNFY SPSKQSQFNN
     INSAFKSTND KLSINDIQYI EAHGTGTKTG DPIETEAISM AFKNRDKSAP ILIGSIKSNI
     GHCEAGSGVA SLIKCCLMFK YQCFLPNIHF KNPNPLIKFN EWNLKVVTSP IPFNKRNNEK
     PVSMMINNFG VTGSNCCLLI SEFKNNNNFK ENINLESQSV NDRVLIPFSA NSSNSLNQYQ
     SKFKNIINNQ FNFIDFTAIQ IYSKSNYLYQ RSVVIASNSN ELFENISNKK QIQTKNSIIS
     NMSFKGKNPI TIFVFSGQGS QYPKMALELY NNEVIFKKSI DLIDSKLSKY YGFSVWEKVK
     TIKDDDLTSI HDPIFAQPAL CMISVSLFEL YYHWGVNPSF ILGHSLGEIS ASYCSGMIDL
     DTFCYTVYQR SIAQSKTNGC GRMLSINISD EEFKSMYSQK YPQIEIACYN SPQSIVVAGN
     ESILNEISKE LKEKEIFTAM LGSLSSFHTS SQQSTKDSIL QLNIESNQPK VPIFSTVTTN
     LFNESNRFNS QYVYDNIIKP VKFTQTISNI YKHIESNQLD NDIVFIEIAP HPTLSFYIKQ
     MVPSSLNESV SVYSALHKKK NDVEEFQQTI SNLYCQNGYN INFKCQFNNK KSNLNIELPL
     YQWSDELYFA QNQVLEQHRK GGPPIDHLGL SNSYYSPFKN SYKTLIDINY KPFQYLKGHM
     VKGKYYFPGC GYIDNIIQLY KNQDIFISFI EFKTPLILIE GINQYLQTNI QQTGKSEYRA
     QFHFKDHKSN EWIQSSNSNF QLLDHGNDIP SNYNIKEIIK NKCNLSKLTK NELYKNIKSK
     TGLNYTGVFQ GVTECYIGDN CTLSVVSLES QTNSFLNIPI LDTCLHGMLI LINDQCQIVF
     DKAIGFKYYS SNIPADFKEN KDSFYVYSNL RPRVGGDSYH GTIIVMLSDG SVLYEIEEVV
     CKSLIPIKDS LKIEYPNDEL YKVHLQSKDS PIPTPSSFKS IIYENDFFQS SLNIPEDLFK
     YISTLFYKDI IKRCPEININ KINSHSVNEI ISSFSKISKH ERLFRFVFET IKENGILNSF
     EEKDDTYFEF NKVIIKSSRI ISKLLFPLEN DNDNEDLPQS LFQNGLMDKI YKCSYLRKKN
     QVISHVIKHS IKEIINNNII IRILEFGGGT ASLSVEVIEE IVTLLQENPN YQVEIEYTWS
     DISPAFIADA KNKINKIIND AAITNGLNVI YHPLTIGESL IETQSIKPSY YDFVIMSNVL
     HVVKDIKQAV EQMYQLLTTN GQLVFLEPPY KSVLNDSIVG SFEQWWSFTD TDIRKDRCGM
     PQQSWYQLLN SCNFKDIVMS KECIFFGSVI QAQKPPISLL NSQPKYDNII IYGGSINSSF
     VENIKLDSNS KSLFQIETIQ EFNKLISKST ITNDSIVYFI KTLETLSLDN FKQITLEYIE
     INQKLLQINS LCKHVLIVSD SRKTNYLASS AIGAARYFDE FPLLKLHTLD FDYDSTQNYI
     NSKNNKMVQF INILTDSKTN VHKEMIIINN KVYYEIVQKE KNLKLKYNSE SFENQNNLMC
     SLSPNLEYQL QSKQIKLRDN QVEVKTIATG INYKDYLNFS GSNSNGDDNT GLPQFGYEFS
     GIITRVGNNV KDYKVGDNVF GLSNSCTSSH IVTNFKKIQI KPSKISHIEA SSIPIDYLTS
     FMSLFNVGSL NIEDNESILI HLGRDGFGLS TFEILKWKGF KSNLFVTVNS DKTKQYLLKK
     YGDLITGIYS NTDKSYVAEI KNKLIKLGSK KKGVDLILNT LPSDFMDSNF KLLTKYGRII
     DLNSNHLNQS EFLKNINFKY NHGYHNFELS LFQKNKILKC LNEISNAIEN GELKTIPIKE
     FTNLNIKDAI KYITNGNIEK ITVSHDHEIY SDIIYRYLDE KEFSILKSNY QINSNNLGKN
     ILITGQSGII LEILKWIIKY SNINTIENVI ILSRSSLKWE LELLINQTKL SNNNIKFHFK
     SVDVGDSEQV DNAINDILNE NQQIRNIDSI FHFAFQQIAC KVQEINMKHL NISHGAKSMG
     AINLHNQSIK RNWKLINFVM ASSALSFIDS TDQCTYACAN TLLDSFSKYR VSLGLPSTCI
     NLGLIESTGF VSKNESISVF LDGNGIIPTP INRVLGLLDL QIQNASKFTN SMISNFKPSK
     FKNNQQISLF LKFDYLMNLK NNSEQTKKEN TGNKNIDELF IEKVSELFSM DESKINKNLR
     LIDYGADSLI IVQLKNWIDK EIGINLITIQ QLQNNTINIS IKMILNSLMK NNQNKYLPSN
     RIDYWKNEMK FEESIKPIPN EIRSRNNNSG KIILLTGTTG FLGGFLLFNM LRLDSCKLIY
     CLIRNKSKSS YPLDEIINNL KYHQLYEKLN KSQISKIIPI IGDLSMNKLG LSNDDYETIS
     KNVNLIINPG ADINQKSSYQ DCKLVNVNGV KEIIKLSLSS LKQRIPIVNF SSFSVFFNQS
     LDKNFDESVL PSIDNIDNLP TEYMKSKVVG EYILLEASKN YNIPSILIRP PSIFLNPETG
     IGHSSDLTLL MIQSCYELGY CPNQILNGFI LINTITWLSN NITNIIMNDN CWTNSKMNIY
     NVHGKQIQSS LIIKPLEKHF NCKQINNNDW IDMVNNSNKK SCIKLKSFHS LENIFKSENK
     GYKSNESQSI SLSTKSLLES MGSYNTDLKI TDKMIISHIK HIFK