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PKS22_DICDI
ID   PKS22_DICDI             Reviewed;        2499 AA.
AC   Q54QD3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable polyketide synthase 22;
DE            Short=dipks22;
DE            EC=2.3.1.-;
GN   Name=pks22; ORFNames=DDB_G0284001;
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 pair pks22/pks23 in chromosome 4.
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DR   EMBL; AAFI02000058; EAL65488.1; -; Genomic_DNA.
DR   RefSeq; XP_638811.1; XM_633719.1.
DR   AlphaFoldDB; Q54QD3; -.
DR   SMR; Q54QD3; -.
DR   STRING; 44689.DDB0230076; -.
DR   PaxDb; Q54QD3; -.
DR   EnsemblProtists; EAL65488; EAL65488; DDB_G0284001.
DR   GeneID; 8624335; -.
DR   KEGG; ddi:DDB_G0284001; -.
DR   dictyBase; DDB_G0284001; pks22.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54QD3; -.
DR   OMA; NWIRANI; -.
DR   PhylomeDB; Q54QD3; -.
DR   PRO; PR:Q54QD3; -.
DR   Proteomes; UP000002195; Chromosome 4.
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; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
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; 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; 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   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..2499
FT                   /note="Probable polyketide synthase 22"
FT                   /id="PRO_0000371385"
FT   DOMAIN          2414..2491
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          158..211
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          623..656
FT                   /note="Acyl/malonyl transferases"
FT   ACT_SITE        177
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        633
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2451
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2499 AA;  282695 MW;  DD7EEADA0AEF8D3A CRC64;
     MIEGNIEKNN DNQVAIVGLG LRLPGNSGSP SEFWKNLLGG FDGIVDSNER WSDTFHSMGE
     ISNKNAGLID LEENWHSFEP LFFGINPTDA KQIDPQIKLM LKLTWEAFED ASIDPLKLRG
     TNTSVFVGAA NTDYSFINFE QNEAPINVFN GTLSAFANRI SYCFDLRGTS LTLDTACSSS
     LNAVHLGYES IVNGKSNYSV VAGCNILLNP YITRSFHSIN ITGKSGRCNS FDESADGFVR
     SEGVVVLILK RLSLAIQDGD QIYCVMKGSS SNVDGTFKKT NFFAPSKNAQ STNIKNAFLS
     SNGAMKYQDI DFFELHSTGT QVGDPIEVEA VADIFKNVKQ EPLLIGSVKS NIGHLEPASG
     VASLAKVCLM FKHRQFVKNI HFNNPNPNIK FKEWNVKVCT ETTAFPDRQV SMAINSFGIT
     GSNACVLLSE YIKPSELKNQ TSMKLNEKSK LLIPISTNSK KSLEQFKSKL LEEIDTYSES
     LTFEEFAMFQ VYSKTTKLSQ RSVLIGNDWN DLKIDINEII STKNNKSGNI IKSNDINPPL
     VFSFCGQGPQ YSKMGLNLYE NEPIYKQSMD ILDSILFKYF GYSIIQKLRS INDDPILINE
     PILAQPSIFM IQISLYKLYL HWGITPSIIV GHSLGEVASA FCSGMIDLET ACFVIYKRAT
     IQNKTNGSGR LLAISLNLEE FNNQFSKEYP EIEISCFNSP SSIVVCGNEL DILNISKSLK
     DKQIFNSLLG TSSAFHSSKQ DIIKDEIIES TNHIQSRPPS ITTFSTVTSN KFDKNTPYNS
     SYIFDNLRKP VLFQQTIENI FKHIESNDLG NSVIFLELSP HPTLNHYVKE MIPKNSNYFL
     NKDSISVLSS LNKKKEDINE IQSTISQLYC FGYNVDFSAQ FKSEITSNSF KKCSYLIPHY
     QWDESLFWRE GISSLNNRKN GAPINQLGNK NESSPHISYT SYIDIKEEPF RFLKDHQFRG
     KSLFPGVGYL DIILKLFPNQ DLTIPLLEFK SQFVLTEGVK KTLTTNLYKS AKNEYRATFN
     FKDQTSGKWI QSANSRILMK SLDVTVKKVD VQSIRDQCNW STLKREQLYD LIKNYANISL
     LEPFQRIEEA SYGDNRCLCK VSLDPTSSYD NESFLNICII DTCIHPCIFF DNPASSVFER
     IEHLKIYSSS VPLTAEDRVK QQYVYCYAEL IKQFSDFIYF KTTCFLKDGT VLLHSPLVTI
     ASTLSTKSET DLECPNNQLF SQCLQPKDSI LQSPLILKEH FNQQLQLQQS NIISISTLST
     YLFSILKKRL NNLTVDEFQN NSLEQLIEKY SYVLDEVEVG TIRSNLILLT INFLLTHHKH
     IDQNQVSNFL LNNIPNELLV VDTIVSNKGI SHIGIYQHQL ILDIISKSII PIVNEKIVFR
     ILEIGCGVGE LTKLINDNLE SILNDNPSYN IDIEFVFSDY TDSKVLLIKE RLFNSKKSCF
     FKIIDLNKQL QEQSFSPSYY DLIILSNTTN QIKDIKTSIS FINEILTPNG HLLILDTNFI
     QTSIDEDYYL ENYKQWLSFN YLNSGSGAMK LNQWNQLLIN DLKFNNFICS TGEIEPYLIQ
     VQKPNLSNSI NSVSKEHTSE YDQIIIFGTC DEINIGSSFC GSGGVVPIAI NSIDKFKEHA
     KLQPLTDKSL ILFIESVNLL TVDNFNQVSM NYIEINQHLL KNEISGCKHI LISRNINFET
     SNLFGSSLIG SFRYFCEFNQ LNIYSFEFEG NNILSGGDKL FNIIQELSNS NKHSQNEFSI
     RSDGKIYYER IKLESNLKLK YKSKSYIENK NELVSRLKPD LTFALEAVLP LNPNFVEVKV
     MASGVNFKDF LVYRQLINMA NSNENGDPSK PQFGYELSGI VTKVGKNVTK FKVGDHVMGV
     TFHTFSSSVH VDQDRIELKP SNISWFEASI SLVYLTSYCS LFELGRLGLH GSTETVLIHS
     GSGGIGLSCI DLLQVYGFKG FLFVTVGSEE KKQFLKDRYG NFITEIYSTK NTDYEYLIKE
     KLIELKAPSQ EYGGFSMICV DLIINTLSAD YMDANFNCLS QGGRIIDLSI THMTTTDTTD
     FYKFKNHIGY MTYESVIAGF RKHKHVLKII VDLLASGKLK TIPFNVYPVT KIKEAIESLG
     DRKHIGKNIV NFNDPEGIDL IDCPEFSNNH NFIHRSSNYK IHQDTLGQTI LITGQAGLSD
     TIIKWIREKR SDSIESIIVL SKSPIKFELE RAIGRIRSTN LKIYFKQVDI SDEKLLLKTI
     NQLFEENKDI KPIESIFHNA FSPAECEPLE IDMNHLISSH SAKSMGAYNL HKLSLNWPIK
     QFVLSSSVTS ILGSQRQCGY VASNCFIDAL SRHRKSLNLP CISINWGLLG GGGFAARNDA
     VFKLFELQGL VGISKDLVWG SLDLLLQNQN ESTNKMVASF EFHATCKTYK NHKLSYKLDY
     FLNPIISKES VTDEKEFSIR QDIVDKFASL LSTDQSKLNL DIKVIDYGAD SLLVVEVKNW
     ADNKFTRNIL SMPEIQNSTI NQIINIVTTK VSNLPSKKK
 
 
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