PKS33_DICDI
ID PKS33_DICDI Reviewed; 3127 AA.
AC Q54FN7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable polyketide synthase 33;
DE Short=dipks33;
DE EC=2.3.1.-;
GN Name=pks33; ORFNames=DDB_G0290729;
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).
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 pair pks33/pks34 in chromosome 5.
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DR EMBL; AAFI02000169; EAL62070.2; -; Genomic_DNA.
DR RefSeq; XP_635575.2; XM_630483.2.
DR SMR; Q54FN7; -.
DR STRING; 44689.DDB0235230; -.
DR PaxDb; Q54FN7; -.
DR EnsemblProtists; EAL62070; EAL62070; DDB_G0290729.
DR GeneID; 8627799; -.
DR KEGG; ddi:DDB_G0290729; -.
DR dictyBase; DDB_G0290729; pks33.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q54FN7; -.
DR OMA; GPGPHWD; -.
DR PhylomeDB; Q54FN7; -.
DR PRO; PR:Q54FN7; -.
DR Proteomes; UP000002195; Chromosome 5.
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; 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; 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 Coiled coil; Membrane; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..3127
FT /note="Probable polyketide synthase 33"
FT /id="PRO_0000371393"
FT TRANSMEM 2937..2957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2539..2616
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 177..230
FT /note="Beta-ketoacyl synthase"
FT REGION 660..693
FT /note="Acyl/malonyl transferase"
FT REGION 1369..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2617..2659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2617..2671
FT /evidence="ECO:0000255"
FT ACT_SITE 196
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 670
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2576
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3127 AA; 355901 MW; D2BC830DFBB00588 CRC64;
MKENSYNTSI HSNKVKNYDD ADSSGDVAVV GIGLRFPSGN LKESISKPNQ LFNELLNGLD
GIVSTSERWS DNYCLNGEIV SKFAGLLPLD EWKQFDPIFF AINPSNDNVG SIDPQQRLLL
KCVWEALEDS GIDPISLRGT NTSTFIGSST IDYNNLQKSP FETQNNIFGS TTNSVANRIG
YCFDFRGENL TIDTACSSSS NAINCGYNSI KSNKSNVSIV GGVNFILDPH ISKSFTQLDM
LSPTGKCHTF SSDADGYVRS EGVGIVVLKR LKDAIKDSNN IYCVIKGSSS NIDGNFDKLN
FYSPSKSSQC ENIKLAIKST NGQINESDID YCETHGTGTP TGDPIELEGI SRVFNNKAST
TKTNNNKQVL VGSVKSNIGH TEACSGVASL IKCCIMFKNK LFLQNINFKE PNPLINFKEW
GLKVVTEPIK FNENKSTVML INNFGITGSN VCLILSEFCS DQFRKSNDYH KMEIDNKFNE
KKKYLIPLSS NSSTSLNNYK SSIIKHSNLT PFSSPTSFEG FICNQIKFKS TSLIQKSVII
ASDWNEFQDE SNHIKLENSD NLISNITVEK KKSPLTVMVL CGQGSQYNKM ALSLYDNVPI
FRESVNRFDK ELFKYYGYSV LDKLRSIDDK DLISIHQPIL AQPANVIIQV SLYELYKHWG
VSADIIIGHS LGEISSAYCS GMIDFQTLCY LTYHRSVAQN RTIGTGRMLS VNISSDEFIN
KYQSTTKYKS LEIACYNSPT SIVIAGKEDL LNEITNEFKS NDIFCSMLGL LSSFHTSSQQ
MIKDEVCSLN ISSKQPSIAV FSTVTTNLFN HQTSPFNADY AFNNIRQPVR FTQTITNLYK
HIESNDMGNE ITFIEVSPHP TLQYYLNQMK STQSSYFNNG KNITIYSPLN KKKNDYNEFL
KTISLLYVNN NFDINFKSQL INNSNNHTNQ SNNLPLYQWD DKEYFKLNPS LEKIKNEGPS
IHSLGNNTDS PYPSYQTFID IKKSPFQWLK GHQVSDKFYY PGMGYVHNLL SIYPNQDITI
SSLEFKSPLV LTEGNRQCLQ TTIAPLSKNE FNIKSHYKDQ KTNQWILSSL GNFSLFKHNI
ENNESINIQS LKDKCNFTTI SKQDFYETIR IKTNLTYKGL FQGVKECYIG NNCSLVKVSL
NEIYNQKEYN HLINNSNMNT FFNTAILDTC LHGVLVAVTQ PIVLDRIEAF KFYSSNITSS
NISNNDTIKE LYVYSETRAR TNSQTYSGSI KIILPNGTLL VDIGNVVCTI VGSNPDSTII
CKPPSNEIYT PYLQSKDSII NKPEQFKHLY RVDEFSVKEE DNQLLSIELL LSLFYKHINN
RCPSINLESL ATLEYDQFKQ LYYNSLVNEN LFKFIFEILK KYQNLPKISN NNNNNNNNNN
NNNNNNNNNK NNGYNNYENL YIRTTKVMAK QLFPLKDDDS ITDTPQSLFE IGYLNEFYKN
SNVIQPSNNL LSEIIVETLK PILNEPIVFR ILEAGGGTGS LSLLILEKIC KLLNDNSTTS
IINIEFTWSD ISASFFAEIK EKFSSFTNHN NLNIIYRVLD LEKPLLDQDL KASYYDFVVM
SNVMHVVKKL KPTLNEIHNI LTPNGQLLYI EPPYKSFYYD SIFGCFSQWW PSSDSDIELR
PDRCCMKQEK WINLLNQCNY KDTIMSGNDN LAFLIQTRKP TINEIISEES KSLDQLNSFS
NIILFSNNNN IRNNNNRNKN DSRSSIQNLI SLNQELRHKI VNINNYNEFQ SWITNNQNKD
DCNKTLIIFL KSIESTMNTF NFKEITFEYI QINQLILKLE LSNNFKHLLL SLNSSTDNYL
SSSIIGSARY FHVEFPQLDL LTLNYDNVSI ENNQQLSLIN YLINSDNNIQ IEFTINNNKV
YYERYFKRSN NIKSKLQSES FETNKDNLYI QLNSNLEYQL YSKKDELNSN EVEIEIKATG
INYKDYLMYI GMIGSDLDIK YGKEYEIENG IGIDNPNIGN DFSGIITRLG NNVKKFKVGD
QVCGIGPKAS SSHVIVDFNF IYYKPFNCNH SVSASIPSIY ITSLHSIYSI GNLKSNESIL
IHSAAGGIGI SSLDLLKSKQ HQGYIFLTVG SKDKEEYLTK KYGSLITAIY SSRNKNYVKD
IKNKLIELGE VEQQGVDLIL NTLSSEYMDS NFQCLNLSGR IIDLSITHLT PNDYMTNNHF
KFNMTYSNVE VVDFTSKLIK SYLKKIIKMI NSNKLELSVP IIEYSNNQFK DAIEYINQRK
HIGKIIVNHN QDEFNRVYNN YQSNNNHIIM KHSYDISKLN IGKNILLTGQ TGIVLEILKY
LIKYSNHSIE NIIILSKSKL KWELELLINQ SKFKKDNIIK FHFNQIDIED SNKVNQVLNQ
LELNENITNI DSIIHFAFMN DISDIQQVDM NRLNNTHGAK TIGAINLHNQ SINRSWNIKQ
FIMASSVVSI VGSDRQCCYV SACNVIDSLS KYRHSIGLPS LAINLGAISS TGFISRNNAI
ETMFKSSILN LFSPQLIISS LDLFIQNQHQ YPNYCISDFN FEILPSTLTN QYLSKFDFEI
NIVKKSNQMK SFTGGNGDSN NEIIRSTILN KISELLSIDE SKINEDLQLT QYGMDSLVIV
QLKNFIDNQI GHNIITIQQL QNNKINQSIE IIKSAHNKNN NNNNINNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNNNL VKKEQQSLDE FIKNETKLNE SIISRPYSIK NILNNNNNSK
SIFLTGSTGF LGAYLLTELI KMNNVSKIYC LIRNNSKLTN PIDVIINNLK KHQLIDMNEE
SPKRKTKIND HTGNISNDKL YGNLNSDNSS NNQIKEDQLI KIIPMIGDIS KDKFGLTEQD
YLKLSNECDI IINSAADLNL KSSYEESKIV NINNVNQIIK LSISNNSSQK LIVHFSSLAV
FINHPFEDGE DFEETNIVPS FNSTPVGYIQ CKVISERLLT NAAESRGIPS IIIRPPVLTL
YNIPITIFIA ILIIDIFSNP ITGIGHSNDF ISLLIKSSKE IGYYPNIHKS VFTTPVTTIA
KTTIDLIFNE NSWNQNKSKP ISIYNFNGDS IEMKSFYRVL ENSFKCKEID FYEWIELVSK
SNGKSSKRYS TFHIHKNQNL LITSSKINSL FKMSNSTKEL LISIGSYNHQ DWEINESIIL
NDIINNH
