ID   PKS42_DICDI             Reviewed;        2655 AA.
AC   Q54D44;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable polyketide synthase 42;
DE            Short=dipks42;
DE            EC=2.3.1.-;
GN   Name=pks42; ORFNames=DDB_G0292544;
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 pks42/pks43_ps in chromosome 6.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000190; EAL61251.2; -; Genomic_DNA.
DR   RefSeq; XP_629652.2; XM_629650.2.
DR   AlphaFoldDB; Q54D44; -.
DR   SMR; Q54D44; -.
DR   PaxDb; Q54D44; -.
DR   EnsemblProtists; EAL61251; EAL61251; DDB_G0292544.
DR   GeneID; 8628717; -.
DR   KEGG; ddi:DDB_G0292544; -.
DR   dictyBase; DDB_G0292544; pks42.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q54D44; -.
DR   PhylomeDB; Q54D44; -.
DR   PRO; PR:Q54D44; -.
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; 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   Coiled coil; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..2655
FT                   /note="Probable polyketide synthase 42"
FT                   /id="PRO_0000371399"
FT   DOMAIN          2517..2594
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          167..220
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          634..667
FT                   /note="Acyl/malonyl transferase"
FT   REGION          1700..1719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2612..2655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2618..2655
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2619..2655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        644
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2554
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2655 AA;  302636 MW;  E3B1FAE3E3D61146 CRC64;
     MIESQREFNC IGGDNQNGVA VIGVGFKIPL DLENCLSSPS ELYSALFNEF DSVTKNTSSR
     WSDNYFKNGD IVSLSAGLLP LREIKSFDPT FFGINPSDAD LIDPQQRLLL KCVWNALEDG
     GIDPISIRSS DTSVYIGCST IDYFLLNRNP VDPHNHGIQT ASYSIPNRIS YCFDFRGESL
     FVDTACSSSL NAVHLGYNSI INLKSKLSIV GGSNLILDPQ NSIFFSKQQV NGPSGKCNSF
     SEEADGFVRS ETVGVVVLKN LKDAIKDGDR IYCVIQGSNS NVDGNYEKLN YISPSKLSQA
     ENITKALKST NGAVNASDID YFECHGTGTP TGDPIELEGI SIALNRTQQS TTLSNPLLIG
     SIKSNIGHGE ASSGIASLIK CCVMFKYRQF LPNINFKTPN PLIKFKEWNL KVVTEPVPFN
     NNKQTIMAIN NFGVSGSNCC IILSEYKSNN NNNNDFKATT HLKSKKFIIP FSSNSSTSLD
     NYKSLLSNET NNFQDFVIKQ INNKSTSLIQ RSVIIASNWS EFNESSNEIQ SNIKKSIISN
     ITIKKKNAVT VFVFCGQGSQ YNKMALSLYE NEHIFKSTMD KLDKELSKHY GYSILEKLRS
     ITDEDLVTIH QPILAIPVNV MVQVSLYELY KHWGIKSDIM VGHSFGEIAC SYCSGMVDFK
     TLCYLTYHRS VAQNKTIGSG KMLSINIGAK EYLDSYSTKY PSVEIACYNS ETSIVIAGNE
     ELLNEISKDL KSKDIFTAML PSLSAFHTTH QSVIKDDICS LNFKSTLSKI TVFSTVTSNQ
     FGINNNNNNN NNQLNSNYLF QNVIQPVKFS ETISNIYKYI ESNDMGNEIT FIEIAPHPTL
     QYYLNQMKSQ QSEYFNNGEK ISIYSACNKK KNDYNEFLKT ISTLFVNGYN NINFKSQIIN
     NNNNDNNNNF NLPLYQWDDN EYYKIHPTWK KANKNGPSIN HLGNLNDSSI KSFKTYINTR
     KPQFQWLKGH SLKGKVVFPG MGYISNLLSV YNMNQDITIN EIQFKSAFIL VDGVNNCLET
     SIVPLTKNEF NIKFHFKDLK TNKWVLCANA NYSLFKHNDN NDKLDIEKLK SNCNYTIISK
     DELYNNIRAK SGLIYKGLFQ GVKEAFIGNR CSLTVLSLNE IENQQEFKHL LENRNFNSLF
     NTAILDSCLH GSLHSKEQSQ IYFDKCEGFK YYSNNINLAT SKRNEYKEIN VYIETNPVIN
     STVIVSLKIM LPDGTLLIEI QKVVCKSSIP IIDSTSVIQP SPKDLHTPYY QPKNSLIKPP
     QSFKHLHCMK EFASIESDNR EMVYMSIYHL IFKAINARSP TKINLESLEN LTLDQFKELI
     KDSAANIQRS NQFIYECLKL YHTNHSNYKK NQIKDFIKEC EDFNGYNQII FKTIKIYAKS
     LFPLPDDDPF TDTIQSLFED DQLENVYIHL KHLYPVNNLL SEIVFQSIKP IINQTSTFRI
     LEIGAGYGTI SQLIFDKLEQ LLADNFTSSR IDIEYTFTDI SNTFLPRAKE RYSKYKRFNI
     IYKLLDLELP LTEGIQDFRP LYYDIVVMSN VLHVVKDINF STNEIYKVLK QNGQLIFVEP
     TYKNLYLDTI FGIFPQWWSF NDDIRTDRCC LEPSKWFEFL ETINFKDTII LGQDNKEILK
     NVENSIILVQ TRKPSQLELS INNSPSTNQF KSFENIILYT DDNQQPNDCS EIIDLLKSLE
     LPIKIINNID QFNQIIKTQY NNNNNNNNNN NNNNNNNNNN TNNNLIIFLK SVNQLNTNNY
     KDITFEYVQI NQILVKLELE ENYKLLLITN NSQSSNYLSN SLIGTSRYLF ADIVSSKLDI
     ITIDFDTVSI KNHQNVISVI NHLLDSKDNS EREYYIINNE INIERYKNES NIKHQLKSKT
     FQENKDELMV QLDSNLEYRL KSKSKQELKS THVEIQVKAI GINYKDYATY SGLIDSIIEI
     DKDKEKDENY DQNYPSIGND FSGVITRIGS DVRKFKVGDE VCGLAPKTSA SHIITEEGYL
     CKKPSNISHS EAASSVTVYT TSFQSIYSIG DLKKNETILI HSGSGGIGLS ALEILKWKNH
     QGYIFATVGS EDKVKYLTDT YGSFITGIYS SRDKDYQDQI KEKLKSLGCD IDHQGVDLIL
     NTLSVEYMDS NFKCLNQKGR CIDLSITHLT PFDYMDYNKF KFNVSYGNIE LVVLPSKIIK
     DHLKKMLKAF SLGSLRFIPI VEFSNLNIRN AVEYINQRKH IGKIVVKNDV DFINKLFIEQ
     QQQQNSVENN EILMKDKYDI SNLELGKNIL LTGQTGIILT ILKWLYKHSN NSIENIIIIS
     KSKLKWELEL FINESTNNRI KIHYKQADVG NNNELNQCFE ELRLRHSIED INSIFHFAFI
     NDIGQFEDVN MNRMDIAHHA KAIGSLNLHN QSIERKWNIK QFVLASSALS VFGGDNQCCY
     ISACSVLDSL SKYRKSIGLP SLSINFGGVT STGFVSRSGA VEANLESSII NLITPQSLIS
     SLDLFIQNSQ TFSNYTHFNF IYDNIESYSL NRMLFKFDYL INQHSSLVSN KRLGGINENN
     NIGDLLVSKI GELLSIEPSK LNLDFRLVDY GLDSLVIVQL KNFIDKQFQP HLISILQLQN
     NKISTTIEII IKGYNNNQNK KIKNEQSNDI PSVVQKETIK DNNENKDDIK IDMDDKKENL
     KGKKENIDDK KENNN