ID PKS30_DICDI Reviewed; 3075 AA.
AC Q54FQ2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Probable polyketide synthase 30;
DE Short=dipks30;
DE EC=2.3.1.-;
GN Name=pks30; ORFNames=DDB_G0290701;
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).
RN [3]
RP FUNCTION.
RX PubMed=18164290; DOI=10.1016/j.yexcr.2007.12.002;
RA Nagasaki A., Uyeda T.Q.P.;
RT "Screening of genes involved in cell migration in Dictyostelium.";
RL Exp. Cell Res. 314:1136-1146(2008).
CC -!- FUNCTION: Probable polyketide synthase (By similarity). May be involved
CC in the process of cell migration. {ECO:0000250,
CC ECO:0000269|PubMed:18164290}.
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; EAL62085.1; -; Genomic_DNA.
DR RefSeq; XP_635589.1; XM_630497.1.
DR SMR; Q54FQ2; -.
DR STRING; 44689.Q54FQ2; -.
DR PaxDb; 44689-DDB0235263; -.
DR EnsemblProtists; EAL62085; EAL62085; DDB_G0290701.
DR GeneID; 8627786; -.
DR KEGG; ddi:DDB_G0290701; -.
DR dictyBase; DDB_G0290701; pks30.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q54FQ2; -.
DR OMA; NYGPEFQ; -.
DR PhylomeDB; Q54FQ2; -.
DR PRO; PR:Q54FQ2; -.
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:0048870; P:cell motility; IGI:dictyBase.
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 CDD; cd05235; SDR_e1; 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; 3.
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; 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; 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 PANTHER; PTHR45681:SF5; POLYKETIDE SYNTHASE 27-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; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 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; 3.
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..3075
FT /note="Probable polyketide synthase 30"
FT /id="PRO_0000371390"
FT DOMAIN 26..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 963..1269
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2533..2610
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 663..696
FT /note="Acyl/malonyl transferase"
FT REGION 963..1085
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1102..1269
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 198
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 337
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 381
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 673
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 997
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1174
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2570
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3075 AA; 349549 MW; 034D04EA30186AD2 CRC64;
MVQNTDNNTY NQLIRDINDY DDAGSSGDVA VIGIGLRFPS GSLKESISKP NQLFNELLNG
LDGIVTTSER WSDNYFLNGE IASKFAGLLP LDEWKQFDPI FFAINPSNDN VSSIDPQQRF
LLKCVWEALE DSGIDPISLR GTNTSTFIGS STIDYNNLQK SSFETQNNIF GSSTHSVANR
IGYCFDFRGE NLTIDTACSS SSNAINCGYN SIKSNKSNVS IVGGVNFILD PHISKSFTQL
GLLSPTGRCH TFSSDADGYV RSEGVGIVVL KKLKDAIKDS NNIYCVIKGS SSNIDGNFDK
LNFYSPSKSS QYENIKLAIK STNGQINESD IDYCETHGTG TPTGDPIELE GISRVFNKAP
ATTNNNHKQV LIGSIKSNIG HTEACSGVAS LIKCCLMFKN KLFLQNINFK EPNPLINFKE
WGLKVVTEPI KFNENKSTVM LINNFGVTGS NVCLILSEFK NNLSRYGNGN GYHKMEIDNN
LNEKKKYLIP LSSNSSTSLN NYKSSIIKHS NSNSSPTTTS FKEFVYNQIK FKSTSLIQKS
VIIASDWNEF QDESNQIKLN NSDNLISNIT VEKKKSPITV MVLCGQGSQY NKMALSLYDN
EPIFRESVNR FDKELFKYYG YSVLDKLRSI DDKDLISIHQ PILAQPANVI IQVSLYELYK
HWGVSADIII GHSLGEVSSP YCSGMIDFQT LCYLTYHRSV AQNRTTGTGR MLSVNISSDE
FINKYQSTTK YKSLEIACYN SPTSIVIAGN EDLLNEITNE FKSNDIFCSM LGSLSSFHTS
SQQMIKDEVC SLNISSKQPS IAVFSTVTTN LFNHQTSPFN ANYVFDNIIQ PVYFTQTITN
LYKHIESNDM GNEITFIEVS PHPTLQYYLN QMKSTQSSYF NNGKNITIYS PLNKKKNDYN
EFLKTISLLY VNNNFDINFK SQLINDNNNI SNTTKLNNLP LYQWDDKEYF KLNSSLEKIK
SEGPSINNLG NNTDSPYLSY QTFIDIKKSP FQWLKGHQVS DKFYYPGMGY VHNLLSIYPN
QDITISSLEF KSPLVLTEGN NQCLQTIIAP LSKNEFNIKS HYKDQKTNQW ILSSLGNFSL
TKHNSITSNK LINIQSLKDK CNFTSMSKQD FYETIRIKTN LTYKGLFQGV KQCYIGNNCS
LAIVSLNEIY NQKEYNHLIN NNNMNTFFNA AILDTCLHGS LVAVTQPVVL DKIEAFKFYS
SNIPLLNKNN NNNNSDDDSI KELYVFSDIK PRTNSQTYSV SVKVILPNGT LLVDISNVVC
ALVSLGSNPD STIICKPPSN DIYTPYLQLK DSIINKPEQF KHLYSVDEFS VKEEDNQFIS
NELLLSLFYK HINNRSPSIN LESLTTLEYN QFKQLYYNSL ANENLFKFIF ENLKRYSNIL
NHDNNHSNIK SKHEELYIRT TKIMAKQLFP LKDDDSITDT PQSLFESGFL DDFYKNSRVV
QPLNNLLSEI IVETLKPILN EPIVFRILEA GGGTGSLSLL ILEKICKLLN DNSTTSIINI
EFTWSDVSAS FFAEIKEKFS SFTNHNNLNI IYRVLDLEKP LLDQDLKASY YDFIVMSNVM
HVVKKLKPTL NEIHNILTPN GQLLYIEPPY KSFYYDSIFG CFSQWWPSSD SDIELRPDRC
CMKQEKWINL LNQCNYRDTI MSGNDNLLFL IQTRKPTINE IISEQSISLD QLNSFNNIIL
FCNNNNSNDK NRNSCSSSIL DLIRSNQELK HKIININNYN EFQSWITNNQ NKDDCNKTLI
IFLKSIESTM NTFNFKEITF EYIQINQLIL KLELSNNFKH LLLSLNSSTD NYLSSSIIGA
ARYFVEFPQL DLYILNYDNV SIENNQQLSL INYLINPNNN IQKEFTINNN KVYYERYCRR
SNNIKSIFQS ESFETNKDNL YIQLNSNLEY QLYSKKAELN SNEVEIEVKA NGINYKDYLM
YIGMIGTDLD IKYGKEYEIE NGIGIDNPNI GNDFSGIITR LGSNVKKFKV GDQVCGIGSK
TNSSHVIIDF NFIYYKPLNY NHSVSASIPS IYITSLHSIY SIGNLKSNES ILIHSAAGGV
GISSLDLLKS KQHQGYIFLT VGSKDKEEYL TKKYGSLITA IYSSRNKDYV YEIKNKLIEL
GVVEQNQQGV DIILNTLSSE YMDSNFQCLN MSGCIVDLSI THLTPNDYMT NNHYKFNMGY
NNVEVVDFPS KLIKSYLKKI IKMINSNELE LSVPIIEYSN NQFKDAIEYI NQRKHIGKII
VNHNQDEFNR VYNNYQSNNN QIIMKHSYDI SKLNIGKNIL LTGQTGIVLE ILKYLVKYSN
HSIENIIILS KSKLKWELEL LINQSKFKKD NNIKFHFNQI DIEDSNKVNQ VLNQLELNEN
ITNIDSIIHF AFMNDIGDVQ QVDMNRLNNA HGAKTIGAIN LHNQSINRSW NIKQFIMASS
IVSIFGSDQQ CCYVSACSVI DSLSKYRHSI GLPSLAINLG AISSTGFISR NNAIETMFKS
SILKLFSPQL VISSLDLFIQ NQHQYPNYCL SDFNFEVLPS TLTNHFLTKF DYQINISKKL
SQIKSSSSGN GGDNNEIIRS TILNKICELL SIDESKINED LQLTQYGMDS LVIVQLKNFI
DNQIGHNLIT IQQLQNNKIN QSIEIIKSAH INNNKNKNNN NNNNLVKKEQ QSLDEFIKNE
IKLNESIISR PYSIKNILNN NNNKSIFLTG STGFLGAYLL TELIKMDNIS KIYCLIRNNS
KLTNPIDVII NNLKKHQLID MNKESPNQRL TKIINRTGNM SNDKLNSNIE NSENNNKQIS
EDQLIKIIPM IGDVSKDKFG LTEQDYLKLS NECDIIINSA ADLNLKSNYE ESKTVNVDSI
NQVIKLSVSN NSSQKLIVHF SSIAVFINHQ LKDGETFEET NILPNFYTTP IGYIQCKVIS
EKLLTNAAES RGIPSIIIRP PDIFSNPITG IGHSNDFVSL LLKVSKEIGY YPNIHKPIFT
TPITTIAKTT IDLIFNENSW NQNKSKPISI YSLNGNSIEM KSIYEFLENK FNCKEIDYQE
WIKLVSKSNG KSSKRYSAFH IHDNQNLLIS TFKINSLFKM SNSTKELLIS IGSYNHQDWE
INESIILNNI NSNSN
//
