PKS32_DICDI
ID PKS32_DICDI Reviewed; 3101 AA.
AC Q54FP8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable polyketide synthase 32;
DE Short=dipks32;
DE EC=2.3.1.-;
GN Name=pks32; ORFNames=DDB_G0290709;
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 -!- 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 quartet pks29/pks30/pks31/pks32 in
CC chromosome 5.
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DR EMBL; AAFI02000167; EAL62089.1; -; Genomic_DNA.
DR RefSeq; XP_635593.1; XM_630501.1.
DR SMR; Q54FP8; -.
DR STRING; 44689.DDB0235258; -.
DR PaxDb; Q54FP8; -.
DR EnsemblProtists; EAL62089; EAL62089; DDB_G0290709.
DR GeneID; 8627790; -.
DR KEGG; ddi:DDB_G0290709; -.
DR dictyBase; DDB_G0290709; pks32.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q54FP8; -.
DR OMA; WECVAEF; -.
DR PhylomeDB; Q54FP8; -.
DR PRO; PR:Q54FP8; -.
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; 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 Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..3101
FT /note="Probable polyketide synthase 32"
FT /id="PRO_0000371392"
FT DOMAIN 2550..2627
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 180..233
FT /note="Beta-ketoacyl synthase"
FT REGION 664..697
FT /note="Acyl/malonyl transferase"
FT REGION 1209..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2627..2648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 674
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2587
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3101 AA; 353160 MW; E91B966152AE408B CRC64;
MVQNTDNNTY DQLIRERNDY DDDAGSSGDV AVIGIGLRFP SGSLKESISK PYQLFNELLN
GLDGIVSTFE RWFDNYYLNG EIVSKFAGLL PLDEWKQFDP IFFAINPSND NVSSIDPQQR
LLLKCVWEAL EDSGIDPISL RGTNTSTFIG SSTIDYCNLQ KSPSETQNNI FGSSTHSIAN
RIGFCFDFRG ESLTIDTACS SSSNAINCGY NSIKSNKSNV SIVGGVNFIL DPHISKSFTQ
LGLLSPTGRC HTFSSDADGY VRSEGVGIVV LKKLKDAIKD SNNIYCVIKG SNSNIDGNFD
KLNFYSPSKS SQCENIKLAI KSTNGQINES DIDYCETHGT GTPTGDPIEL EGISRVFNTT
KISSATTITT NNNNKQVLVG SIKSNIGHTE ACSGVASLIK CCLMFKNKLF LQNINFKEPN
PLINFKEWGL KVVTEPIKFN ENKQTVMLIN NFGVTGSNVC LILSEFKNNH YGNDYHKMKI
DNKFNEKKRY LIPFSSNSST SLNNYKSSII KHSNSSSTTT SFKEFVHNQI KFKSTSLIQK
SVIIASDWNE FQDESNQIKL NSSDNLISNI TVEKKKSPLT VMVLCGQGSQ YNKMALSLYD
NEPIFRESVN RFDKELFKYY GYSVLDKLRS IDDKDLISIH QPILAQPANI MIQVSLYELY
KHWGVSADII IGHSLGEVSS AYCSGMIDFE TLCYLTYHRS VAQNRTTGTG RMLSVNISSD
EFINNYQSTT KYESLEIACY NSPTSIVIAG KEDLLNEITN EFKSNDIFCS MLGSLSSFHT
SSQQMIKDEV CSLNISSKQP SIAVFSTVTT NLFNHQTSPF NANYVFDNII QPVYFTQTIT
NLYKHIESND MGNEITFIEV SPHPTLQYYL NQMKSTQSSY FNNGKNITIY SPLNKKKNDY
NEFLKTISLL YVNNNFDINF KSQLINNNNS NNNYENQLNN LPLYQWDDKE YFKLNSSLEK
IKSEGPSINN LGNNTDSPYP SYQTFIDIKK SPFQWLKGHQ VSDKFYYPGM GYVHNLLSIY
PNQDITISSL EFKSPLVLTE GNNQCLQTII TPLSKNEFNI KSHYKDQKTN QWILSSLGNF
SLTKHNSIIS NKLINIQSLK DKCNFTSISK QDLYETIRIK TNLTYKGLFQ GVKQCHIGNN
CSLAIVSLNE IYNQKEYNHL INNTNMNSFF NAAILDTCLH GSLVAVTQPV VLDRIEGFKY
YSSNIPSFKN GNNNDDDEES NNNNNNNNNN NNNNNNNIKE LYVFSDIKSR TNSQTYSISV
KIILPNGTLL VDISNVVCTL VSLPNPESAI ICKPPSNDIY TPYLQSKDSV INKPEQFKHL
YRVDEFSVNE EDNQFISNEL LLSLFYKHIN NRCPSINLES LTTLEYNQFK QLYYNSSVNE
NLFKFIFENL KRYSNILNHD NNHSNIKSEN EELYIRTTKI MAKQLFPLKD DDSITDTPQS
LFESGFLDDF YKNSRVVQPL NNLLSEIIVE TLKPILNEPI VFRILEAGGG TGSLSLLILE
KICKLLNDNS TTSIINIEFT WSDISASFFA EIKEKFSSFT NHNNLNIIYR VLDLEKPLLD
QDLKASYYDF VVMSNVMHVV KKLKPTLNEI HNILTPNGQL MFIEPPYKSF YYDSIFGCFS
QWWPSYDSDI ELRPDRCCMK QEKWINLLNQ CNYRDTIMSG NDNLVFLIQT RKPTINEIIS
EQSISLDQLN SFNNIILFSN NNNSNDKNRN SCSSSILDLI RLNQELKHKI ININNYNEFQ
SWITNNQNKD GCNKTLIIFL KSIESKMNTF NFKEITFEYI QINQLILKLE LSNNFKHLLL
SLNSTTDNYL SSSIVGAARY FVEFPQLDLY ILNYDNVSIE NNQQLSLINY LINPNNNIQK
EFTINNNKVY YERYCRRSNN IKSIFQSESF ETNKDNLYIQ LNSNLEYQLY SKKDELNSNE
VEIEIKANGI NYKDYLMYIG MIGSDLDIKY GKEYEIENGI GIDNPNIGND FSGIITRLGS
NVKKFKVGDQ VCGVGSKTNS SHVIVDYNYI YYKPLNYNHS VSASIPSIYI TSLHSIYSIG
NLKSNESILI HSAAGGIGIS SLDLLKSKQH QGYIFLTVGS KDKEEYLTKK YGSLITAIYS
SRNKDYVYEI KNKLIELSVV EQHQQGVDLI LNTLSSEYMD SNFQCLNLSG RIVDLSITHL
TPNDYMINNH YKFNMGYNNV EVVDFPSKLF KGYLKKIIKM ANSNKLELSV PIIEYSNNQF
KDAIEYINQR KHIGKIIVNH NQDEFNRVYN NYQNNNNHII MKHSYDISKL NIGKNILLTG
QTGIVLEILK YLIKYSNHSI ENIIILSKSK LKWELELLIN QSKFKKDNNI KFHFNQIDIE
DSNKVNQVLN QLELNENITN IDSIIHFAFM NDIGDVQQVD MNRLNNTHGA KTIGAINLHN
QSINRSWNIK QFIMASSVVS IFGSDQQCCY VSACSVIDSL SKYRHSIGLP SLAINLGAIS
STGFVSRNNA IETMLKSSIL NLFSPQLVIS SLDLFIQNQH QYPNYCLSDF NFEILPSTLT
NHFLKKFDYQ INIVKKSNQI KSSSGGNGGD NNEIIRSTIL NKISELLSID ESKINEDLQL
TQYGMDSLVI VQLKNFIDNQ LGHNIITIQQ LQNNKINQSI EIIKSANNKN NKNNNNNNNN
KTNKNNNNLV KKEQQSLDEF IKHETKLNES IISRPYSIKN ILNNNNNKSI FLTGSTGFLG
AYLLTELIKM KNVSKIYCLI RNNSKLTNPI DAIINNLKKH QLINMNKESP NQRSSKILNH
TGNISNDKLS IIENSENNNK QIREDQLIKI IPMIGDISKD KFGLTEQDYL KLSNECDIII
NSAADLNLKS NYEESKTVNV DSINQVIKLS VSNNSSQKLI VHFSSIAVFI NHQLKDGETF
EETNILPNFD TTPVGYIQSK VISEKLLTNA AESRGIPSII IRPPDIFSNP ITGIGHSNDF
ISLFLKVSKE IGYYPNIHKP IFTTPVTTIA KTTIDLIFNE NSWNQNKSKP ISIYSLNGNS
IEMKSIYEFL ENKFNCKEID YQEWIKLVSK SNGKSSKRYS AFHIHDNQNL LISNFKINSL
FKMSNSTKEL LISIGSYNHQ DWEINESIIL NNINNNNKEI K