ID   PKS44_DICDI             Reviewed;        3078 AA.
AC   Q54B51;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable polyketide synthase 44;
DE            Short=dipks44;
DE            EC=2.3.1.-;
GN   Name=pks44; ORFNames=DDB_G0293902;
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 pks44/pks45 in chromosome 6.
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DR   EMBL; AAFI02000224; EAL60450.1; -; Genomic_DNA.
DR   RefSeq; XP_628865.1; XM_628863.1.
DR   SMR; Q54B51; -.
DR   STRING; 44689.DDB0230077; -.
DR   PaxDb; Q54B51; -.
DR   EnsemblProtists; EAL60450; EAL60450; DDB_G0293902.
DR   GeneID; 8629480; -.
DR   KEGG; ddi:DDB_G0293902; -.
DR   dictyBase; DDB_G0293902; pks44.
DR   eggNOG; KOG1178; Eukaryota.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54B51; -.
DR   OMA; HYDFTDV; -.
DR   PhylomeDB; Q54B51; -.
DR   PRO; PR:Q54B51; -.
DR   Proteomes; UP000002195; Chromosome 6.
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; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 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..3078
FT                   /note="Probable polyketide synthase 44"
FT                   /id="PRO_0000371400"
FT   TRANSMEM        2694..2714
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2558..2636
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          156..209
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          627..660
FT                   /note="Acyl/malonyl transferase"
FT   REGION          2087..2108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2080..2119
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2087..2106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        637
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2596
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   3078 AA;  348031 MW;  33A1B448C478ECE6 CRC64;
     MENQNIKYGD NDVAIIGIGL RLPNSINKPL ELWEGLLAGF DGIVETTNRW SDSFSAMDEI
     SSKYAGLIDL DEWMSFDPLF FGIIPTEVPS IDPQQRLLLK CTWEAFEDAN IDPFKLRGTN
     TSVYVGASSL DYASINVDFD ETPMNIFNSN MSGISNRISY CYDFRGTSLT IDTACSSSLN
     AVHLGYKSII NGESDYSIVG GCNFIMSPHT SRSFESINVT SKTGKSKAFD QDANGFVRSE
     GVVSIILKKM SKAIQDGDQI YSVIKGTNSN VDGNLNKGNF FAPSKQSQAN NIKSAMESCN
     KETTNSTPIA LNDIDFFELH GTSTQIGDPI ECEGVSSVFK ESREKPLLIG SIKANIGHLE
     PASGVASLAK VALMFKHRQF VKNINFDKPN PNIKFDEWKI KVCTENTPFP NNKKVSIAIN
     SFGITGSNAC LILTEYIKPK TTTTTTANNN GNQKYLIPIS ANSKSSLESY KEKLINSSKE
     FSETINFKDF VKYQLDSKTL KLTQRSVIIA SNWEEAGSTQ SIVTTNTNRS GNIIKDANKN
     PQLVFVFSGQ GPQWSKMFTQ LYDQEPIFKQ KTDQIDSLLS KHYGYSILNK LNSIKDDDTV
     TINEPILAQP SVFMIQMALI ELYKHWGILA SISIGHSLGE VSSAVCSGMI DLETGCFIIY
     HRSRLQQQTV GSGRMLVASL NEQQFNQEFQ QKYPSIEISC FNSPFSIVLA GKESELQEIS
     NILKEKETFS IFLSTQSSFH SSSQEPIKDE LLKQLKDIKS TKSNIPNFST VTSNLFNDND
     DDEVVQQPDE ASSHNSTTTL FDSNYVYENV RKPVQFEKAI KNVFNYIEKK GLGSSVIFLE
     ISASPVLGNY IREMIPQDSN YFFIEDQTIS VLSSLNKKNK DQVLEIQTSI SQLYCKGYNV
     NFNCSNQTKS LDFKNTGYKQ LSDVLFKYSW DDESYWSVSP LISNYIKNGP ATNHLGYRNE
     RQPYQSFTSS IDIKKEPFEF LKGHSSRNRV IYPGCGYIDS ILKAFPDQDL TIQSMEYKSA
     ILLSSSMKTY LSTNIIPSGK NEYRVSFHYK DKKTNKWILS CSGRLSTTKH NDEVVKKVDI
     EKLKSKCNFV TIQKKELYET IKYKAQLTLE GKFQSIEEVS YGHNCCLSKV PLTTLSSYDN
     ESFLNLCVID AAFQPLGAVK ENQEPMVFAS IENLKFFSKN IPKSAEDREK YKFVYTYTQV
     KEKKCGSYFV SILTMLQDGT ILFFSPLVVY TQLTPYKNQY IIESPNDNLY KICYQSKDST
     LPHPLLLKDK FDQPRFETTD KQSQVIKKAL SNCLFAIFKR NNNLFTKVEV KSQSIDYLIE
     KYCLIIDNDD DNDGIDDNSI LVNGGVASID DMVLASTTGK ETTIVNNGKR SLAKLIFQIL
     KSNVDLIDWN NIATYTKNIS KQQLNIIQAI GNLIVTPLSV TNQVTESDLI SKTQLDIINN
     RMKIKQYELI SNTIATDLIK PIINNSILFR ILEINSGFGY LSEMIINKIN QLLIEFESSY
     EIEIEFTFTL NGTNQDDNKE ISNSIKEKLT NLLISKSSIS IIFKELNLNE SFLEQKFNPS
     YYDLIVLTNL STITNLNESI EFINSILYPN GHLIIIDTKN QSNFQDYEIF EQFLIFDNFG
     GGIVDDNIDW VKIFQDNNIN RVVATPNIKP HVIQVQKSKL YEKVMGTLDD ITGPYDQIII
     IGYQLQGTDE DNFQSPIMDI NKQGTDIYRI KTIEEFEKHC STIPPTDKSI LFFISAMNNL
     SLENYKQVNF DYIKINQYLL ANKLGSLFIL ATKSALKEST NALAASLIGS FRYFSEFSNI
     LNLYSFDFGE DVYTLSKEIS LKWLNMAIDL LDPNKHIQRE YIFRNGNETW FERIGKIKRV
     KSKYQSKSYL DDKEDSLVAR LDQNLEYQLE AKQSNLKENE IEVQVVATGI NFKDSLIFRN
     LVPPVLANHE GDFSKPEFGF ECSGIVSRIG SKVKKFKVGD SVLGISWKST SSHAINYQDA
     FVLKPDNISF VEAASIPIVY CTSFYSLFYS GNLSIKNNES VLIHQASGGI GLACLNILKS
     CGFKSKLYVT VGSKEKEDYL RETYGDFITG IYSSRNTDFL ENIKTDLSNK NDNNNNNNNN
     NNDNKESNIK ELLDNDDDEI LPFIHKKGVD LIINTLPFEF LDTNFLLLGQ GGRIVDLSVT
     HLNNNDTTDF SKFKWFIGYS TVEIFYNGFE KSKHILQLIT DMIKNKELPL IPIKEYPINQ
     IKDAIDFIGQ RKHIGKIVIN HKLGLRDGCS NLVQDTIKSL QNHLKDNYLV ASPDFKFMGD
     SLGKTILLTG QTGLSLSIAQ ACLLNNYQDL EGIIVISKSP IKHELQYLIS LAKYLSRKTR
     VHFKQADCSK FDEMRKVISE IYEKDDPKLS PVESIFHNAF VPVMSEPQDI DMKHIDDAYD
     AKTTGAMNLY MLMSMYDWKL KNFFFSSSIT SVSGSSRQAG YCGANLVLES MAKVIQSQGI
     RCSTICWGII GDTGYVSRNE SVAKFLNGLG NAPMPLNMVL GSLDLLLQQP TLSTDTTIIA
     SFDFNNLPKL SRDGSNNISY KFDYFTNPIQ SNQNNCSSDD LSIREQILAK FSEFLSVDDQ
     SKINLDIKLL DYGADSMVIV ELKNYLDKTY TPNILSIQQL QNITINQLIQ SVTDAMNKLN
     GNENKSIKKS NKLVQQKQID WVKEIKLDSS IKPTDEMIKL FKQLQQQAST TTSNTVFLTG
     SSGFIGIYIL FYLIKSVNCK IVYCLIRRKT IEEATTFLIE FLKVHQLYNQ LTTDEINKIK
     PVLGDYTLDS FGLSVDQYTN ISNNVDLIIN SAASVNYQMG YEDSKVESVE GVLQCLRFSC
     HNKLKKLFQV STLGIYSDDK RDNLDDYTFA QIDPKIIQSK NSIINGYLQG KIVSEYHIKE
     AANRGIPCCI IRLPFIGPNP NTGVGRDLDL FQTLFQSCYA MSTYPKQESG LQFYATPVTW
     AAQNLSFISL NPKCWSTSSN HPSSISENLT CYSLFGESIC FNVLLTELAT QLKWKPTSSG
     EFLKKLRSFP NEPSCKKLHI VLKNTKNLLL NVYIPGNYKL NPTLKQLLQS NNTYEGWKIT
     PEMILTHLSF IFKKKLNK