ID   PKS41_DICDI             Reviewed;        2542 AA.
AC   Q54ED6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable polyketide synthase 41;
DE            Short=dipks41;
DE            EC=2.3.1.-;
GN   Name=pks41; ORFNames=DDB_G0291684;
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 pks40/pks41 in chromosome 6.
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DR   EMBL; AAFI02000177; EAL61826.1; -; Genomic_DNA.
DR   RefSeq; XP_635304.1; XM_630212.1.
DR   AlphaFoldDB; Q54ED6; -.
DR   SMR; Q54ED6; -.
DR   PaxDb; Q54ED6; -.
DR   PRIDE; Q54ED6; -.
DR   EnsemblProtists; EAL61826; EAL61826; DDB_G0291684.
DR   GeneID; 8628248; -.
DR   KEGG; ddi:DDB_G0291684; -.
DR   dictyBase; DDB_G0291684; pks41.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54ED6; -.
DR   PhylomeDB; Q54ED6; -.
DR   PRO; PR:Q54ED6; -.
DR   Proteomes; UP000002195; Chromosome 6.
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; 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; 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; 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; 2.
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..2542
FT                   /note="Probable polyketide synthase 41"
FT                   /id="PRO_0000371398"
FT   DOMAIN          2459..2537
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          158..211
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          628..661
FT                   /note="Acyl/malonyl transferase"
FT   ACT_SITE        177
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        638
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2496
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2542 AA;  288536 MW;  D281219899617A16 CRC64;
     MDSKNLVDEN CNKVAIIGIG FRFPNLKGDI TPNELWSKLL NRYDGIVKND RWNESFFKSG
     DISTNYAGFI PFEELKSFDP LFFGINPSEG IHMCPQQRLL LKCTWEALED SGIDPIEIRG
     SNTSVFIGCS GADYQNLNKN DNKVQQEIFS SSTHSISNRV SYCFDLHGES MTIDTACSSS
     SNAIRRGYKS IIDGSSNISV VGGINILLDP NISKSYSRLN ILSKDGKCKS FDAGADGYVR
     SDAAGIAILK NLNDAIKDDN NIYCVIDGSA SNVDGNGFSD KSNFYSPSKS SQVECIRLAL
     ESTNGQVNEN DIVYFEAHGT GTPTGDPIEL ESVSIALKTS ENRSSDNPLL IGSFKPNIGH
     TESASGISSL IKCCLILKNQ CFVPNLNFNK PNPLIKFDQW NLKVVTDPID FSTLNYINKR
     VSIAINNFGV TGSNCCLIVS SFKGNQIRNN INNKSKSPKQ YLIPFSTNSI KSLDLYKSRI
     DNNVEFKEFA ENQIKSKSKK LIQRSVVIAS NWDEFNLKSN TINTSNDKLT SNMLVSSNKK
     NVTMVFVFCG QGAQYSTMAK NLYDNEPIFK KSMDKIDSKL NEYYGFSILE KLRSFNENDL
     KGIQYSIIAQ PSTCMVQISL FELYCHWGIK PSIIVGHSLG EISSSYCSGM IDLDTFCYLI
     YHRSMVQSKT NGLGRMLSIS IGENEYNSKY SSRYPELEIA CYNSPSSIVI AGKELILNEI
     IKELKKDGVF CAILGSPTSF HTSSQLSVKD EILKISFKSK QPTIPIFSTV TTNLYDEMNP
     FDTKYVYDNI INPVRFTNTI SNIYKHIELN YSVNNNSNEV IFIEIAPHPT LSFYLKQMVP
     EDKKQSVSIF SPLSKKKSND LFEIQKLISE LYCLGYNGIG FNIQLSDHNN TNNQTRVNLP
     LYQWEDQEYW KLDNLHQYHL SNGPSINHLG ISNSNHTPIK SYQTHINIQK KPFQWLKGHQ
     IKGKYYFPGC GYIDNILKIF GESKTDTNPN KELPDILISF IEFKTPLIFM DGISQCLQTN
     IHSTGKKEYK ALFHFKDEKS SSDWVQTSTA NFQLFSRGPN LNEDDEQSLF MYNINDLISN
     QCNLTKLSKQ ELYSHIKTKC GLNYSGDFQR VDKCYLGYNC SLSEISIIQG VNENRSTFFD
     SSIIDCCLHG SIGLIDENCQ LVFEKLEELT YYSSKVPKTT SQHSKIYVYS KLKPRIGDSY
     SASIIVMLEN GTVLFEMENA SFKSTTKIKD PLAMEYPTNE IYSCNLQSKD SLIPSLSSFD
     HIFKRKIPNE YVDQINIYES FIPKLLFSNI NKRCPEITID EIQSSEIEQL LLKYYKIKED
     NDNKWLSRLF TFAFESIKQW YHNEDYDFEN VLSPHNFKIF SKSTKIISKL LFPLENDNDE
     DSPQSLFEGG LLDKFYSSGF SAQNELVGEI IQESIKPILN EKLVFRILEF GGGVGSLSLL
     VLEKINSLLI QYPNYQIDIE YTWSDISPSF ITEAKAKFEK FNDRFNIIYK ALNLEQPLIG
     EKQGLKPQYF DYIIMFNVLH VIKDVKYGVE QIYQLLVPNG HLLFIEPIYK SIIGDGIFGV
     FDQWWSFQDT EIRKDRCCMK QKTWYKLLKS VNFNDDIRMT PELTCFVIQA QKPSISNLSF
     SKSETTNYDS IIVFGNKYAS NLSNHFIKSI DNGNLQFIST IEELNKIGKY ISNESIIYFI
     KSIDELSVDN FVNITHEYTQ INQKLMELNC KCKHVLITND STTTNYLSSS LIGAARYYHE
     CPLELFILNF DTPSIIENQN LFKTIEPLIN SSINIQREFI INNHKVYYER IKNETKLKSI
     FKNSSSFESL EQVDNFMISL TPNLEYKVKV KPTSILKENE VEIKVMSTGL NYKDYLIYAG
     LVESVEPIFG IEFSGIITRI STGSKEFKVG DHVYGIGKST TSSHIITDID VISHKPSNIS
     HSEASSIPVV YLTSYHSLYN IGALKNNETI LIHSATGGVG LSTLEILKWK GHSGLIFVTV
     GSNEKEEYLR ENYGDMISGI YSTRNKNFVK QIKSKISKLN PFGKSGVDFI LNTLSSSDYM
     DSNFKCLNMS GRIVDLSITH LNSNEFTDNK KFKYNYGYHN IELQYVDKKI IKSTLSIISN
     AVSSNDLQLI PITHYSIEKV KESIEFINER VHMGKIIINH ENQDSIINEL IEKQKSINKF
     DQSIFKQNYK LEPSLLGRNI LLTGQSGIVL EILKWILRNS ENNSIGNIII LSKSSIKWEM
     EYLINKVKLI NKLGNFFNNI KFHFKSVDIS DSGLIDESIN KLLIENPDIN NIDSIFHFAY
     TQATCNSDEV DLHHLTQSHS AKSMGAINLH NQSIKRNWKL KNFIMSSSVS SKTSTANQCG
     YISSNNVLDA LSKYRISIGL PTICTNYGLI ESTGFVSRNE SVAALLSGEG FIPISANLIL
     GTLDLQLQNQ AQSSNLILSN FNFTSLNGLP QKSLISKFDY QININEENEK SKSLLKDDNV
     ELTVDQLITF KISEILSTDI LKLNKDIILV DYGIDSLVII QLKNWVDKEF SIPNELTIQK
     IQNSTINSFI QLVKNSMDKN KK