PKS23_DICDI
ID PKS23_DICDI Reviewed; 2499 AA.
AC Q54QD1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Probable polyketide synthase 23;
DE Short=dipks23;
DE EC=2.3.1.-;
GN Name=pks23; ORFNames=DDB_G0283931;
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.
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; AAFI02000058; EAL65453.1; -; Genomic_DNA.
DR RefSeq; XP_638813.1; XM_633721.1.
DR AlphaFoldDB; Q54QD1; -.
DR SMR; Q54QD1; -.
DR STRING; 44689.DDB0230074; -.
DR PaxDb; Q54QD1; -.
DR EnsemblProtists; EAL65453; EAL65453; DDB_G0283931.
DR GeneID; 8624337; -.
DR KEGG; ddi:DDB_G0283931; -.
DR dictyBase; DDB_G0283931; pks23.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q54QD1; -.
DR PhylomeDB; Q54QD1; -.
DR PRO; PR:Q54QD1; -.
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 23"
FT /id="PRO_0000371386"
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; 283071 MW; A0FACB3F4056C9AB CRC64;
MIEGNFEKNN DNQVAIVGLG LRLPGNSGSP LEFWKNLLDG FDGIVDSNQR WSDTLHSIGE
ISNKNAGLID LEENWHSFEP LFFGINPTDA KQIDPQIKLM LKLTWEAFED ASIDPLKLRG
TNTSVFVGAA NTDYSLINFE QNEAPINIFN 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 YIKPSEIKNQ TSMKLNEKSK LLIPISTNSK KSLEQFKSKL LEEIDTYSES
LTFEEFAMFQ VYSKTTKLSQ RSVLIGNDWN DLKIDINEII STKNNKSGNI IKSNDINPPL
VFSFCGQGPQ YSKMGLNLYQ NEPIFKEFMD LLDSILFKYF GYSIIQKLRS INDDPILINE
PILALPSIFM IQISLYKLYL HWGITPSIIV GHSLGEVASA FCSGMIDLET ACFVIYKRAT
IQNKTNGSGR LLAISLNLEE FNNQFSKEYP EIEISCFNSP SSIVVCGNEL DILNISKSLK
EKQIFNSLLG TSSAFHSSKQ DIIKDEIIES TNHIQSRPPS ITIFSTVTSN KFDKNTPYDS
NYIFDNIRKP VLFQQTIENI FKYIESNDLG NSVIFLELSP HPTLNHYVKE MIPKNSNYFL
NKDSISVLSS LNKKKEDINE IQSTISQLYC FGYNIDFSAQ FKSEITSNSF KKCSYLIPHY
QWDESLFWRE GISSINNRKN GASINQLGNK NELSPHISYT SYIDIKEEPF RFLKDHQFRG
KSLFPGVGYL DIILKLFPNQ DLTIPLLEFK SQFVLTEGVK KTLTTNLYKS AKNEYRATFN
FKDQTSGKWI QSANSRILMK SLDVTVKKVD VQSIRDQCNW STLKREQLYD LIKNYSNISL
LESFQRIEEA SYGDNRCLCK VSLDPTSSYD NESFLNICII DTCIHPCIFF DNPASSVFER
IEHLKIYSSS VPLTAEDRVK QQYVYCYVEL IKKYSDFIYF KTTCFLKDGT VLLHSPLVTI
ASTLSTNIDT NIECPNNQLF SQCLQPKDSI LQSPLILKEY FNQQLQLQQS NIISISTLSS
YLFSTLKKIL NNLTTDEFQN GSLEEFIGKY SYILEEIQEA STFRSNLIFL SINFLLTHHK
HIDQNQVSNF LLNNIPNELL VLDTIVSNKG ISHIGIYQHQ LILDIISKSI IPIVNEKIVF
RILEIGCGVG ELTKLINDKL ESILNDNPSY NIDIEFVFSD YTDSKVLLIK ERLFNSKKSC
FFKIIDLNKQ LQEQSFSPSY YDLIILSNTT NQIKDIKTSI SFINEILTPN GHLLILDTNF
IQTSIDEDYY LENYKQWLSF NYLNSGSGAM KLNQWNQLLI NDLKFNNFIC STGEIEPYLI
QVQKSNLSNS INSVSKEHSS EYDQIIIFGT CDEINIGSSF YGLVPIAINS IDKFKEHVKL
QPLTDKSLIL FIESVNLLTV DNFNQVSMNY IEINQHLLKN EISGCKHILI SRNVNFETSN
LFGSSLIGSF RYFCEFNQLN IYSFEFEGNN ILSGDGGDKL FNIIQELSNS NKHSQNEFSI
RSDGKIYYER IKLESNLKLK YKSKSYIENK NELVSRLKPD LTFALEAVLP LNPNFVEVKV
MASGVNFKDF LVYRQLINMA NSNENGDPSK PQFGYELSGI VTKVGKNVTK FKVGDHVMGG
AFHTFSSSVH VDQDRIELKP SNISWFEASQ SLVYLTSYCS LFELGRLDLY GSTETVLIHS
GSGGIGLSCI DLLQVYGFKG FLFVTVGSEE KKQFLKDRYG NFITEIYSTK NTDYEYLIKE
KLIELKAPSQ EYGSFSMICV DLIINTLSAD YMDANFNCLS QGGRIIDLSI THMTTTDTTD
FYKFRNHIGY MTYESVIAGF RKHKHVLKII VDLLASGKLK TIPFNVYPVT KIKEAIESLG
DRKHIGKNIV NFNDPEGIDL IDCPEFSNNH NFIHPSSNYK IHQDTLGKTI LITGQAGLSD
TIIKWIREKR SDSIESIIVL SKSPIKFELE RAIGRIRSTN LKIYFKQVDI SDEKLLLKSI
NQLFEENKDI KPIESIFHNA FSPAECEPLE IDMNHLISSH SAKSMGAYNL HKLSLNWPIK
QFVLSSSVTS ILGSQRQCGY VASNCFIDAL SRHRKSLNLP CISINWGLLG GGGFAARNDA
VFKLFELQGS VGISKDLVWG SLDLLLQNQN ESTNKMVASF EFHATCKTYK YHKLSYKLDY
FLNPIISKES VTDEKEFSIR QDIVDKFASL LSTDQSKLNL DIKVIDYGAD SLLVVEVKNW
ADNIFARNIL SMPEIQNSTI NQIINIVTTK VSNLPSKKK
