ID PKS24_DICDI Reviewed; 2471 AA.
AC Q54KU5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Probable polyketide synthase 24;
DE Short=dipks24;
DE EC=2.3.1.-;
GN Name=pks24; ORFNames=DDB_G0287119;
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=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 pks24/pks25 in chromosome 4.
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DR EMBL; AAFI02000096; EAL63924.1; -; Genomic_DNA.
DR RefSeq; XP_637425.1; XM_632333.1.
DR AlphaFoldDB; Q54KU5; -.
DR SMR; Q54KU5; -.
DR STRING; 44689.Q54KU5; -.
DR PaxDb; 44689-DDB0230081; -.
DR EnsemblProtists; EAL63924; EAL63924; DDB_G0287119.
DR GeneID; 8625958; -.
DR KEGG; ddi:DDB_G0287119; -.
DR dictyBase; DDB_G0287119; pks24.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q54KU5; -.
DR PhylomeDB; Q54KU5; -.
DR PRO; PR:Q54KU5; -.
DR Proteomes; UP000002195; Chromosome 4.
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; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 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.
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; 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; IPR049551; PKS_DH_C.
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 PANTHER; PTHR45681:SF4; POLYKETIDE SYNTHASE 14-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; PF13602; ADH_zinc_N_2; 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; PF14765; PS-DH; 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 Coiled coil; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2471
FT /note="Probable polyketide synthase 24"
FT /id="PRO_0000367830"
FT DOMAIN 21..449
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 953..1245
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2336..2413
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 654..687
FT /note="Acyl/malonyl transferase"
FT REGION 953..1075
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1094..1245
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT COILED 1426..1469
FT /evidence="ECO:0000255"
FT ACT_SITE 190
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 332
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 372
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 664
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 987
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1157
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2373
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2471 AA; 280910 MW; C78993A055394DB1 CRC64;
MKQNKINKAE ILQVDDKHVE ENLVAIVGVG FRLPSGSIEN ERNNTPQTLW NNLINGFDGV
VKTSERFNDN FFKNHEIANN YSGLLPLDEV KSFDPLFFGI NPNEAPTIDP IQRLLLKCTW
EALEDSLIDP ISIKGTDTSV FIGCTESDYH NINKNEVKSN VFSSLNHAIS NRISYCYDLH
GNSITLDTAC SSSLNAIALG YDSIKNKKSK MSIVGGVNIL LDSYFFKAYS SLNILSKSNG
RCKSFDASAD GYVRSECIGV VVLKNLKDAI KDGNRIYCTI NGASANVDGI GYSDKSNFYS
PSSISQSENL KNAIQSTNGT VKPSDIDYVE AHGTGTPTGD PIEVEGISKV FKDTRSTDTP
LLIGSFKSNI GHCEAASGIA SLIKCCLMYK NKCFAPNIHF KTPNPAIKFK EWNLKVVTEP
IPFNKFKNTS MVVNNFGATG SNCCLVLSQF NYNTINNNIN NHNNNHNHNH NHNNIKINNY
LIPFSANSVE SLKKYQSLII ENKEYESQYS FEEFVKNQIY NKSTSLYQRS VIVAKDWNDF
NNVENQVKYQ TSSSTSSNIT ITNKNNNPIT VFVFCGQGSQ YNTMALELYK NEKVFRNSMD
MLDNKMKNYF GYSILEKLRA IQDSDKCSVH EQTMAQPSTV IIQVSLYELY KHWGIKASFM
LGHSLGEVTT AYCSGMIDID QLCYLIYHRS TLQIRTNGSG KMLSINISSD EYKTNYMSRY
PTIEIACYNS PSSIVIAGNE QILNEISKEL KEKEIFSAML GSLSSFHTSS QNIIKDDILN
LNIQSSQPVI PTFSTVTSNL FNESTIFDSE YFFDNISKPV SFTQTISNLY KHIEDNQIGS
NIVFIEIAPH PTLSFYLKQM IPKQSQYFRN GESISVYSTL HKKKNDVEEF QKSISQLFCD
DAYDINFKCQ FNNINSNIEA ISNFNLPLYQ WDDQHYWLNK SIEHKNNLIG PPISILGNSM
QDSNPFIKSY QTIIDTGKDA FKYLKGHNVS DKCYFPGTGY IDNIFKLYPN QDLTINSIEF
KVPFVLTDGI GQCLQTNVYQ TGKSEYRAQF HLKDEMNNQW INTSNSNFHL NSNDNYHEEK
QKLDIQDIKQ TKCNLSSIPW DEFYSLMKTQ LGANFYGIFS KVVECYIGDN CSLTEISLEL
PENFHDEQSF FNCPLIDACF HGTVILYIQK NCKIVTDKVE GLRYYASNIP KNRDEHSSIF
IYSTLKSSPS DDLLSSSIVV MLEDGTVIIE VDNLVVKSLT PVKDPLLIET PSDFIYTPYL
QSKDSQIQSP LEFKSIYQNN QVDDGLLIPN VVIETIKPLI NRKMEFRILE FGGNNLSKST
LLLNEINSLL EENPHYEIDI EYTWSDNNSS ILKDAKLELS KVDKGYLSIL YRSLGLDVDN
SLLEKQKLNP SYYDLIIVSN ISNLTKDIEY SLNQIYQILT PNGYLIINEQ QQQQQQQQQQ
QQQQQQQQQQ LLNNENNKES LKNLLVNCNF NSDIMIKSSS ISDSDIKSII IQAQKPSLKL
QPKTINTFDQ VILYCYQDEQ LQQQQLINKF ENHYNNCKII KVSTIEEFYK LSTTITNNSI
IYFIKSIEQL TLENFKSVTF EYVQINQKLY ELKSKCTHVL ITCDSQSSNY LSSSVLGAAR
YFDEIPTLQL FTLDFDKDSL TNDLDLFKTI DYLINPKNNI QREFYIKNSG TVYFEMYKKE
LKNLKNSYKS ESYHDLSKQQ DQLVSKLDEH FEYQLNSKQI DLEPYEIEVK VKATGINYKD
YLKYNEMIKV NEAGIGFDFS GVVSRVGIKS SKEFKVGDQV YGIAYETSSS HIIIDSLLAC
HKPSKITHVQ AASIPAVYST SLYCLYDVGN LRDEESVLIH SGSGGVGLSG LEILKSNNHS
SPIFVTVGSE EKKQYLINTY GDLITGIYST RDTNYQKQIK NKLIELGYET HGVDLIINTL
SSEFMDTNFK CLNPKGRIVD LTTTHLNPNE FIDNSRYRYN IGYNSIEILK VGKSTIKKLL
QSISKSIENE TLNALIPITE FSNSNIKKSI ESIKERKHVG KIVISHDTDI IDKLIEKESM
IDYSILKSDY KIKNLGKNVL VTGQTGLILE VLKWITKYNS TVENIIILSK SSLKWELEFL
MNYNNNNNNN NNNNKIKYHF KKCDISNWNL INKTIDQVLK DNPTITNIDS IFHFAALQIN
KKLKDIDMNS LNVSHSAKTF GAVNLHNLSI KRDWKIINFI LASSVVSVLG SFDQCSYVSA
CCVVDSLSQY RKSIGLPSFT INIGGVSDRG YLSRHKLVEA VLGGQGVELI SPNQLLGTLD
LQIQNPNMPT NAFVNNFNWP LFKSFKQKLH QKFDFILNPI NVDNSISMEN DTNQSSSSTN
VKNKFLNKVS ELLSIDPSKI NTNIKMINYG ADSLITVQLK NWVDKEWSPH LITIQQIQSN
SIGMVYQIIN DSLDKKKKEM DEKLLPITAK TTTTTKNDPN DKTEYKYIAG GDCCREFSIK
FHYSSVVNFI I
//
