PKS13_DICDI
ID PKS13_DICDI Reviewed; 2551 AA.
AC Q559A9; Q86IG0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable polyketide synthase 13;
DE Short=dipks13;
DE EC=2.3.1.-;
GN Name=pks13; ORFNames=DDB_G0272981;
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; EAL71128.1; -; Genomic_DNA.
DR RefSeq; XP_644907.1; XM_639815.1.
DR AlphaFoldDB; Q559A9; -.
DR SMR; Q559A9; -.
DR STRING; 44689.DDB0230082; -.
DR PaxDb; Q559A9; -.
DR PRIDE; Q559A9; -.
DR EnsemblProtists; EAL71128; EAL71128; DDB_G0272981.
DR GeneID; 8618586; -.
DR KEGG; ddi:DDB_G0272981; -.
DR dictyBase; DDB_G0272981; pks13.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q559A9; -.
DR PhylomeDB; Q559A9; -.
DR PRO; PR:Q559A9; -.
DR Proteomes; UP000002195; Chromosome 2.
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 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; 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; 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; 2.
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 Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2551
FT /note="Probable polyketide synthase 13"
FT /id="PRO_0000376886"
FT DOMAIN 2465..2542
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 157..210
FT /note="Beta-ketoacyl synthase"
FT REGION 621..654
FT /note="Acyl/malonyl transferase"
FT ACT_SITE 176
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 631
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2502
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2551 AA; 288907 MW; D4A5898486F564C6 CRC64;
MENFKYRNNE NDVAIIGIGF RLPGCKNFTP NELWNNLKNG FNGVVELSNR WSDNFYTMGK
VSSAYAGLLP FDELKSFDPL FFGINPTEVP TIDPQQRILL KCTWEAFEDA GIDPIKIRGS
NTSVFIGTST NDYQRIIREK DQTITNAFGT SLHATSNRIS YCFDFRGPSM TLDTACSSSL
NCVKLGYQSI RDGTSNLSIA GGVNLIIDPY FTASISDLNI LSKTGSCKTF DASADGFARA
EGSGIIVMKN LKQAMIDGDK IYCVIKGASS NVDGGGLQDK SNFYAPSSLS QCNNIKMALK
STNGTVEPKD ISYFECHGTG TPTGDPIETR GISMVFNDES RSKENPLLIG SIKSNIGHLE
AGSGIASLIK CCLMFKNKCF APNINFKVPN PKIKFEEWNL KVVTEPIQFT KSNTCIGLSN
FGVTGSNCCL ILSQFNNNNN DNQIVGNNNN IKSNKEYLIP FSSNSVKSLE NYQQLLIKNG
ENEFKFLEFI KHQIFTKPTS LYQRSVVIAS SWDQFNNAKI MKTSNSKSSN ISIERNNPIT
VFVFCGQGSQ YDRMGLELYN NDFIFKESMD LLDNKLSKYY GYSVLEKLRN CDSKSIQHPM
IAQPVMCMFN ISLFELYKHW GIEVSFIIGH SLGEIPAAYC SGMINIDTLC YLIYHRSIAQ
TKTHTNGRML SINISADEYF SQYSKQYPDI EIACFNSPTS IVIAGNEQKL NEISEILKEK
GIFSAMLASL SSFHTSSQNK VKEDIVNKQF DSKQSEIPIF STVTTNLFDS VTSPFNSSYV
FNNIVSPVKF SQTISNLYKH IESNQLGNDI VFIELAPHPT LQFYLKQMIP KPTNDDNSIE
FKVSVYSALN KKNNDIEEIQ RTISQLYCDN GYNVNFKCQF QHDDTHGSIN SNINQLSNIS
LPHYQWDDEK YWKEDPSISK LIVNGPQTDN LGYLNENSPN SKSYETFIDI KRPPFQYLKG
HMVKGKYYFP GCGYIDNLLK IYKSQDLTIN QMGFKSPLIF IEGVNQALQT NIFKKSTSNT
TTNNNDEFRV EYHFNDQKTN RWILSSFGDF QLSNHSSNSD NLEKINIKQL IQNQCNLTKL
SRDELYSHIK SKTGLTYNGV FQGVNKCYLG ENCSLSEVSL ELKREPSSFF NTAVLDTCLH
GMLCLLEEQS QLVFDRIEGF KYHSSNVPTS EEEMKIHSNI YVYSTINPSR IGDSYSASIV
IMMEDGTVLI EIENAVCTSL TPIKESISVK YPTNQLFSMY LQSKDSPIPS PLNFKSLYNQ
NQQQLKIDKQ FTDWMQKCEK FISNQFFKNI EKRNPEINLE ILNSKTIIEL KSKYCQNLKN
ERLFQFVFET IKQLGVNAYD DDDDLTIDSS EDRKSIYEIL IKSTKVIPKL LFPLEDEDLT
IDSPQSLFEN GLLDRFYNNP NLMTNQCQLI AQIIKESLKP LLNKKMVFRI LEMGGGTCSL
SVVVLNLINQ LLLENPSFEI DIEYTWSDIS PSFISAAKEK LSHIDKRINI LYRSIDIEQP
FIEKQDLSPS YYDFVIMSNV LHVVKKLSPS LDEIHKILTP NGHLLFVEIP YKELISDSIF
GAFNQWWAFE DTDIRKDRCS IPPNQWIQVL SNHNYKDTIV SDNKECTWCC FVIHSQKPSL
LELSKKIECN QYDNIIVFGN ENSQDNFTKS IKLSYNNNII KWVSNIVEIK KFIKLNIITN
NSIIYFTKGI EELTIDNFKL INFQYIQINQ LLLKYESKCK NVLVTRDCDG SNYLASSLIG
AARYFDEYRQ LELFTLDFDN DTIQSCDECS SSSCSNLIKL IEPLIDPKIN IQREFLIRNN
RVYFERAKLE TNLKKSFKSE SFENSNKLIS TLNFNLDYQL QSKPFKQLLQ NEIEVEIKAT
GINYRDYLVF TGSLPIEKTN HNGISNQPEF GVDFSGIVTK VGGGGGNGEF KVGDRVYGIG
HNTTSSHITI DSRYASLIPN SLDYIEASSI TSSYILSLYG IFDIGNLDIQ DNESILIHSG
TGGIGLSALN SLRWKGHKSH LFVTVSSKEK EQYLRDNYGS FITGIYSNKD KNYPKLIKEK
LNQLGSNKQG VDLILSSLPN GDDNLNFKCL AKNGRIIDLS NNIDLFNISK SKIKKLLNTI
NDGFESGELQ VIPIIEFSNS NIRDAIEFIN ERQHIGKIVI SHDDSNLLID LINKHSNQPN
YSILKSDYQI SQSNLGKNIL ITGQSGIVLE ILKWIIKFSN SIENVIILSK SLMKWELELL
IGKTMKKANN KIKFHFKSVD VSDSIQVENS INQILNDNPN IVNIDSIFHF AFTQITKKVE
EIDMESLNVS HNAKTIGAIN LHNQSINRNW RLNNFVMASS ATSIIGSTDQ CSYVCANTVL
DSLSKYRKSI GLPSICTNYG AIESAGFVSK NESVAAMFNG IGIISISTDL ILGTLDLQIQ
NQQSSTNLML SDFNFLNFVN NNLQLSLISK FDFQTNLAKN QVNEKLQNQT QNQNLQIQSP
SSTTDCQTII KDSFLHKISE VLSIDISKLN LDLKLLDYGA DSLAIVQIKN WIDMEVSPNL
IVIQQLQTFT ITSSIQYTIN SFLKKKVQSQ E
