ID PKS8_DICDI Reviewed; 2514 AA.
AC B0G101; Q86AE5; Q86JI2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 27-NOV-2024, entry version 97.
DE RecName: Full=Probable polyketide synthase 8/35;
DE Short=dipks35;
DE Short=dipks8;
DE EC=2.3.1.-;
GN Name=pks8; ORFNames=DDB_G0271618;
GN and
GN Name=pks35; ORFNames=DDB_G0295667;
OS Dictyostelium discoideum (Social amoeba).
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 and clustered as a quintuplet pks5/pks6/pks7/pks8/pks9
CC in chromosome 2.
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DR EMBL; AAFI02000006; EDR41106.1; -; Genomic_DNA.
DR EMBL; AAFI02000169; EDR41032.1; -; Genomic_DNA.
DR RefSeq; XP_001732964.1; XM_001732912.1.
DR RefSeq; XP_001733036.1; XM_001732984.1.
DR AlphaFoldDB; B0G101; -.
DR SMR; B0G101; -.
DR STRING; 44689.B0G101; -.
DR PaxDb; 44689-DDB0235164; -.
DR EnsemblProtists; EDR41032; EDR41032; DDB_G0295667.
DR EnsemblProtists; EDR41106; EDR41106; DDB_G0271618.
DR GeneID; 8618020; -.
DR GeneID; 8627806; -.
DR KEGG; ddi:DDB_G0271618; -.
DR KEGG; ddi:DDB_G0295667; -.
DR dictyBase; DDB_G0295667; pks35.
DR dictyBase; DDB_G0271618; pks8.
DR VEuPathDB; AmoebaDB:DDB_G0271618; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; B0G101; -.
DR PhylomeDB; B0G101; -.
DR PRO; PR:B0G101; -.
DR Proteomes; UP000002195; Chromosome 2.
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 CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013154; ADH-like_N.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR049900; PKS_mFAS_DH.
DR InterPro; IPR050444; Polyketide_Synthase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF7; POLYKETIDE SYNTHASE 10-RELATED; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2514
FT /note="Probable polyketide synthase 8/35"
FT /id="PRO_0000376883"
FT DOMAIN 11..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 925..1209
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2431..2508
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 635..668
FT /note="Acyl/malonyl transferase"
FT REGION 925..1047
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1064..1209
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 181
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 323
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 362
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 645
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 959
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1122
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2468
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2514 AA; 285291 MW; D1669E848B3A00E3 CRC64;
MNNLEIINLI DKGVAIVGVG FRIPSGNNEN SICSPDDLFN NLKNGFDGVS STSERWSDNF
HKLGEISSPN AGLLPFNECK SFDPLFFGIN PSDAHQIDPQ QRLLLKCTWE ALEDASIDPI
SIRGTNTSVF IGSSNIDYQH INKHQDSVLK NVIAQSAYAV SNRISYCFDF NGPSLSIDTA
CSSSLNAVSQ GYHSILNGTS NMSIVGGVNL ILDVGMIKAY SYLSMLSKTH GKCKAFDESG
DGFTRGECAT IVVLKNLQDA VKDGNRIYCV INGSSSNVDG GGHMDKVNLY SPSKQSQFNN
INSAFKSTNG KLSINDIQYI EAHGTGTKTG DPIETEAISM AFKNRDKSTP ILIGSIKSNI
GHCEAGSGVA SLIKCCLMFK YQCFLPNIHF KNPNPLIKFN EWNLKVVTSP IPFNKRINEK
PVSMMINNFG VTGSNCCLLI SEFKKQDYES YENNNNNKSN HKNILIPFSA NSSNSLNQYQ
SKFKNIINNQ FNFIDFTANQ IYSKSNYLYQ RSVVIASNSN ELFEKILNKK QIQTKNSIIS
NMSFKGKNPI TIFVFSGQGS QYPKMALELY NNDEIFKKSI DLIDSKLSKY YGYSVWGKLT
TIKDDDLTSI HDPIFAQPAL CMLSVSLFEI YCHWGVNPSF ILGHSLGEIS AAYCSGMIDL
DTFCYTVYYR SIAQSKTNGC GRMLSINISD EEFKSMYSQK YPQIEIACYN SPQSIVVAGN
ESILNEISKE LKEKEIFTAM LGSLSSFHTS SQQCTKDSIL QLNIESNQPK VPIFSTVTTN
LFNESNRFNS QYVYDNIIKP VKFTQTISNI YKHIESNQLN NDIVFIEIAP HPTISFYIKQ
MVPSSLNESV SVYSALHKKK NDVEEFQQTI SNLYCQNGYS INFKCQLENK KSNQSINLPL
YQWDDELYFA QTQTLEQYTK EGPPIDHLGL SNSYYSPFKN SYRTFIDINN KPFQYLKGHM
VKGKYYFPGC GYIDIIIQLY KNQDIFISFI EFKTPLILIE GINQYLQTNI QQTGKSEYRA
QFHFKDQKSN EWIQSSNANF QLLDHGNDIP SNYNIEEIIK NKCNLSKLTK NELYTQIKSK
TGLNYTGVFQ GATECYLGND CSLSVLSLKS QTNSFLNIPI LDTCLHGMLV LINDQSQIVF
DKAIGFKYYS SNIPSDLKEY KDSIYVYSNL KPKNADSYHG SIIVMLSDGS VLYEIQEVIF
KSLIPIKHSL KIEYPNDELY KVHLQSKDSQ IPTPSSFKSI IYENDFFHSA LNIPEDLFKY
ISTLFYKDII KRCPEININK INSHSVNEII SSFSKISKNQ RLFRFVFETI KENGILNSLE
ENDDAYFEFN ELVIKSSKII SKLLFPLESD NDNEDLPQSL FQNGLMDKIY KCSYLRKKYQ
MISHVIIHSI KEIINNNIII RILEFGGGTA SLSVEVIGEI VALLQENPNY QVEIEYTWSD
ISPAFIADAK NKINKIINDA AITNGLNVIY RSLTIDESLL ENQAIKPSYY DFVIMSNVLH
VVKNIKQAVE QMYQLLTPNG QLLFIEPPYK SVLIDSIIGS FEQWWSFTDT DIRKDRCGMS
QQSWYQLLKT CNFKDILMSK ECIFVGSVIH AQKPPISLLN SQPKHDNIII YGGGGNLSFV
ENIKLDSNSK SLIQIETIQE FNQLLSQSTI TNDSIIYFIK TLETLSLDNY KQITLEYIEI
NQRLLQINSL CKHVLIVSDS RKTNYLASSV VGAARYFDEF QQLKLHTLDF DYDSTQNYIN
SKNNKMVQFI NILVDSKTNV HKEMIIINNK VYYEIVQKEK NLKLKYNSES FENQNNLMCS
LSPNLEYQLQ SKQIKLRDNQ VEVKTIATGI NYKDYLNFSG SNNNNGDDNT GLPQFGYEFS
GIITRVGNNV KDYKVGDNVF GLSNSCTSSH IVTNFKNIQL KPSNISHNEA SSIPIDYLTS
FMSLFNVGSL NIEDNESILI HLGSDSFGLS TFEILKWKGF KSNLFVTVDL DETKQYLLDR
YGDFITGIYS NTDKSYVTEI KNELIKLGSK KKGVDLILNT LPSDFMDSNF ELLTKSGRII
DLTSNHLNQS EFLKNINFKY NHGYHNFQLS LIQKNKIQKC LYEISHAIEN GELKTIPIKE
FTNLNIKDAI KYITNGNIEK ITVSHDHEIY SDIIYRSLDE KEFSILKSNY QINSNNLGKN
ILITGQSGII LEILKWIIKY SNINTIENVI ILSRSSLKWE LELLINQTKL SNNNIKFHFK
SVDVGDSEQV DNAINEILNE NQQITNIDSI YHFAFQQITC KVQEINMKHL DISHGAKSMG
AVNLHNQSIK RNWKLINFVM ASSALSLIGS TDQCTYACAN LLLDSFSKYR ESLGLPSACI
NLGSIESTGF VSKNESISEF TDGIGYVPTP INLVLGLLDL QIQNAGKFTN SMLSNLISSK
FKNIQQTSLF LKFDYLMNLN DNSEQTKKEN IGNKNIDELF IEKVSELFST DQSRINKNLR
LIDYGADSLI IVQLKNWIDK EIGINLITIK QLQNNTINIS IKMILNSLMK NNQI
//
