ID F0ZWT9_DICPU Unreviewed; 2966 AA.
AC F0ZWT9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGC31599.1};
GN ORFNames=DICPUDRAFT_156533 {ECO:0000313|EMBL:EGC31599.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC31599.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- FUNCTION: Probable polyketide synthase.
CC {ECO:0000256|ARBA:ARBA00037046}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; GL871243; EGC31599.1; -; Genomic_DNA.
DR RefSeq; XP_003291883.1; XM_003291835.1.
DR STRING; 5786.F0ZWT9; -.
DR EnsemblProtists; EGC31599; EGC31599; DICPUDRAFT_156533.
DR GeneID; 10505630; -.
DR KEGG; dpp:DICPUDRAFT_156533; -.
DR eggNOG; KOG1202; Eukaryota.
DR eggNOG; KOG1221; Eukaryota.
DR InParanoid; F0ZWT9; -.
DR OMA; FAGAMFH; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 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; 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:SF1; POLYKETIDE SYNTHASE 2-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; 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; 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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..439
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2461..2538
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2966 AA; 334332 MW; 1A9E57BC68B33C04 CRC64;
MIENNIDISS KSYRDDCDVA IVGLGLRLPG NSNRTSELWD NLLNGFDGIV ETNERWSDTF
NAMGEIASKE AGLLELEEWM SFDPLHFGIN PAEAKQIDPQ QKLLLKTTWE AFEDAGIDPL
TLRGTSTSVF VGASSQDYGI MYMDHSEELV NYNVFNSNLG GFANRISYCF DFRGTSLTVD
TACSSSLNAC TLAYKSIVNG DSDYSIVGGS NLILNPQISK AFTSINIIGK SGRCKAFDES
ADGFVRAEGV AVLILKKLSL AQADGDQIYA VIRGCNSNVD GTLNKGNFMK PSKTAQTNNI
IKAFESTKGS LQYSDIDFFE VHGTGTPIGD PIEVEAVADV FKSVKTPDNP LLIGSIKSNI
GHLEPASGVA SLAKCCLMLK NRQFVKNIHF EKPNPNIKFE EWNVKVCTEN TEFPNNKQVS
VAINSFGITG SNVCILLSEY NNSVVPSKNN TKPTTILIPI SANSKKSLDQ LKDEIIGNST
LYSNTIDFKD FVYNQLYSKS TQLVQRSVFI VSNFSDLSLE TSSISTNSTI SGNILKSNVE
DNEANDNSSK TPLIYVMCGQ GPQWNGQAIE LYNKEPIFKK SMDTIDSILS KYFGYSILSK
LRSIKDNDNN TINEPTVAQP SIFMLQVSLY DLYKHWDIKP SIILGHSFGE VSAAYCSGMI
TLETACEIIY QRSTLQNKTI GSGKMLAIGL NEQQFKDQFS SKYPTIEISC YNSPSSIVIC
GNESEVNEIG QTLKEKQVFS TLLGSPSSFH SSKQEVIKDE IITLTKNIKS NKPNIPIFST
VTGEIFKSED SQFDSNYIYN NIRQPVLFQK AIENIFKYIE SNELGNRVQF LELSPHPTLV
NYIKEMIPTT SDFYQPENIS VLSSLNRKTN TDMIEIRKSI SQLYCNGYNV NFKCQLPAPT
TVEKLQSKKA SYVLPRYKWD DDIYFHQSSS IQTYKMNGST INTLGYKYDQ TPFISYTSYI
DVSQEPYKFL KGHQGKGKTL FPGCGYLDNI LKSFPNQDIT INILEFKSPL ILIDGVRQCL
STNIYQSGKS EYRVLFHYKD IKTGKWILSA QGRFSISKHN KTPKNVDLNV CKNICNWITL
PRKELYEAIK EMAQLNLTGS FQSIEEGKFG NNAAFIKIAL NPLSSYDNQL FLNTCVLDAC
FQSLSVFKDH SSLTFFDRLM EVQFFSENIP RSAMDRDKLK YVYCYTELID RVGDSYIAKV
VMMLEDGTIL FTSPAAVYTA INPNTNGYTI ENPNHCFYSV AKQSKDSPLE PPSKTLSSKI
TEIIPTPANN ILKAITTTLY TPVKKSYQAI TPAGVTEDST QLLISKYFKV SESDGTPKMN
LAKLFFEMLK NNVSLIEYGA SANLAKVVNA QDIKTINKLT KFLLNETPTP IDQASSTLIT
SFIPEIPHNQ IIKEIITASI TPIINEKIVF RILEVGSGIG LLSEIIATEI NSLIEKNPLS
EINIEFTTSD KENTFAPLIK EKLESIVESN LSSFKCLFNT IDFKQDLLDQ NFYPSYYDII
IVSTFSDIED KKSSVEKLNK ILYPNGYLVI IDTLFKPKTT DKELETYGQW LSYNCLNSTT
TIDEWKQLLV TELGFKDVIS TTSQTSLITA QKPKLVESTL SMQLPIADYD QIIIFGLSID
GIDESKLISG INQATEKPDS LYRILSYEDF EKHIESKPLT NKSIIFFVST INDIGQGNFV
EITYDYIRIN QHLLKTKNGC KHILVSKLSQ LESINAFASS VIGAFRYFCE FSELNIYAFD
FGFDIFEKSL TDFRIYNELS NPQKHIQREY IIRNESIYFE RIKQDINLKL KYNSTSYIDK
KEELIARLDA QNLEFKLEAR RSLLENEIEV QVKAVGINFK DSLVYRGLVP KESTNRKGDH
NNPEMGFECS GIVTRVGSNV KKLKVGDQVL GACFSAASSH VIDDEERFLL KPSNISFVEA
ASIPLVYITS YFSLFYQGNL SIDQNETVLI HSGTGGIGLA CIELLKAMGF KSLLFVTVGS
KEKEQFLRNT YGDFITGIYS SRNTDYMHQV RNKISEIRGK EKPVFSDLYF GEHGVDVILN
TLPVEFMEAN FNTLAQGGRI VDLSVTHLHP NETTDYSKFR FLISYSTSEI MSSGFKKSKP
FFETVVNMIK EEKLSLLPIK EYPVSEIKQA IEFISERQHI GKLVVNFETT PDLIQDTIEK
SHHGFEKNYL LPSLTYQVDN NRFGKTILLS GQKGLSLTII KWILVNTPKN LDQAIKNIIV
FSKSPIKFEL EIIMAAAKSK NIPINFYFKQ VDISLSLEVD QAIDQLYKDN PNLEPVESIF
HNAFLPVQSE AEEINLQQLV DSHGAKIFGM MNLYQSVGSK GWLVKKFVLA SSVTSIIGGH
RQCGYVCANV VIDSFTKVLR QFGIPCVSIN FSAIENSGYV SRNESVQALF SSQGLQQIST
NLVLGSLDLI TQNQDQLNGK IVAQFNYSNI GKTFKNNLHL YKIDFFLNSI QSKFGSSYDD
DDEISIRDQI VDKFSEYLSV DKSKINMDVR LCDYGMDSIM VVELKNWLDK TYVPNILTIA
QLQQVTINQL AAAVKNAVSK SNNKKTIKKK QQQTNSSIEW ESEIKLDESF ISPSQNQIKV
YKETLATNKD NQIVLLTGAT GFFGLYLLSD LVKSSDYKKV YCLTRNRSKE EALKTIIQLL
KDHQIYKQLT QDQLDKIQPI SGDYSKDMFG MSKEEYQLLS KEVTTVINSA ADTNLKKKYR
DMKESLDGVN QCLKFTIHYN LKKFIQISTV SVYANSTSTQ TNDEYAFPSI NKESMESVTM
TGYNQSKLVA EYRIKEASSK GVPAMIIRCP PLFPNPETGI GRPFDLFQVL LQSCYLMDVY
PQELMFQKMY TIPITWASRN ISFIISNCWN FSTPIENLIC FNLFGNSIQI GDIIQSLATD
LTWRRLTSLQ FIKKLSIYEN DSCRLLASFV SNQQDFLRNI IVIPGQLNLN DQLKQILESN
NLFNGWEVSK QNIITHLSYT FKKKIL
//