ID PKS16_DICDI Reviewed; 2603 AA.
AC Q869W9; Q554C7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Probable polyketide synthase 16;
DE Short=dipks16;
DE EC=2.3.1.-;
GN Name=pks16; ORFNames=DDB_G0275069;
OS Dictyostelium discoideum (Social amoeba).
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 [3]
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).
RN [4]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
RN [5]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
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 -!- INDUCTION: Up-regulated by P.aeruginosa, PAO1 strain and PA14 strain
CC infection and down-regulated by phagocytic stimuli and growth on
CC bacteria. {ECO:0000269|PubMed:18559084, ECO:0000269|PubMed:18590548}.
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 pks16/pks17 in chromosome 2.
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DR EMBL; AAFI02000013; EAL69815.1; -; Genomic_DNA.
DR RefSeq; XP_643784.1; XM_638692.1.
DR AlphaFoldDB; Q869W9; -.
DR SMR; Q869W9; -.
DR STRING; 44689.Q869W9; -.
DR PaxDb; 44689-DDB0230068; -.
DR EnsemblProtists; EAL69815; EAL69815; DDB_G0275069.
DR GeneID; 8619829; -.
DR KEGG; ddi:DDB_G0275069; -.
DR dictyBase; DDB_G0275069; pks16.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q869W9; -.
DR OMA; RYPWQHG; -.
DR PhylomeDB; Q869W9; -.
DR Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-DDI-199220; Vitamin B5 (pantothenate) metabolism.
DR Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR PRO; PR:Q869W9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEP:dictyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08954; KR_1_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR049011; Anamorsin_N_metazoan.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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 PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF20922; Anamorsin_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; PF21089; PKS_DH_N; 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; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS52019; PKS_MFAS_DH; 1.
PE 2: Evidence at transcript level;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2603
FT /note="Probable polyketide synthase 16"
FT /id="PRO_0000371381"
FT DOMAIN 11..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT DOMAIN 937..1216
FT /note="PKS/mFAS DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT DOMAIN 2506..2583
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 631..664
FT /note="Acyl/malonyl transferases"
FT REGION 937..1057
FT /note="N-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1072..1216
FT /note="C-terminal hotdog fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT REGION 1358..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2580..2603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 316
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 356
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 641
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 968
FT /note="Proton acceptor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT ACT_SITE 1132
FT /note="Proton donor; for dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT MOD_RES 2543
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2603 AA; 290905 MW; 8FE8316C8505F63D CRC64;
MTFNNIKDEN NDDIAIIGMG FRFPGGGNNP DQFWNQLSNK MDGISKISQE KWSRSFYEQK
YINNEYGGVL KDEEWKNFDP LFFGISPKEA PTIDPQQRLL MTTLWEAFED ANIKPSTLRG
SDTAVFIGMM NLDYQRCQFR DISYINPYTV TGSAGSFVSN RLSFSFDLRG PSMTLDTACS
SSLNAVYLGC QAIATGDSKM AIVGGVNGIF DPSISMTFSG LNMLGHKGQC RSFDAGADGY
IRSEGGGVCI LKKYSDAIKD GDRIYCVIKG GSSNVDGYNA KTNITQPSMK AQGENIEIAL
KKSGVNPSDI YYIEAHGTGT PVGDPIEIEA ISRIFKDNHT PDAPLYIGSV KSNIGHLESA
AGIASLIKVA LSLKNRSLVP NIHFEKPNPL IKFEDWNIRV VTDEIQFPTN KLINMGINCF
GLSGSNCHMI LSEAPINYDE LLKTTNNNST SSSSNDDKKE YLIPFSANCN ISLDKYIEKL
ISNQSIYKDT ILFKDFVKHQ TISKSNLIKR KVITASDWDD FLNKRNETTS TSSLTSTISA
PASSTPVIYV FTGQGPQWRD MGKALYETES VFKDAIDHCD KLLANYFGYS ILQKLRSLES
DDSPEIHHPI LAQPSIFLIQ VGLVALYKSF GISPSIVVGH SFGEVSSALF SGVISLETAV
KIVYYRGLAQ NLTMGTGRLL SIGIGADAYL EKCALLYPEI EIACYNDPNS IVITGSEQDL
LGAKSTLSAE GVFCAFLGTP CSFHSSKQEM IKEKIFKDLS DLPESNVPCV PFFSTITGSQ
LSHKGFYNVQ YIYDNLRMPV EFTKAISNIF NFIEENESYK NAIFLEIGPH PTLGFYIPKC
KPSNSTITSK PIIVSPLHKK KEELTQFKLA ISTLYCNGVE IDFASGQQLL PTSSSSGGGD
ISSFKESTNK LPRYQWDFEE YWDEPNQSKM VKRGPSNNLL GHDQFAGNTL MELFIDINKS
AHQYLKGHKI KGKYLFPGSG YIDNILRQFN GQDITIFNLE FSNPFFLKDG VQHHLQTSIT
PTTKGEFKVE FFIKDNRNST KWTKTSNGRI GLFKHNPKNN KLDIEKLKSQ CSFTTLTKSE
VYNKLLLLSL PYGPTFQRVE SCSIGDGCSF FKLSMSPCSE FDKDFLNPSI IDCAFHGLLV
LSEGPQEIVF DRLQDMKFYS SNVPSTRPQF IYAFAKFDKI VGNSTHGSLD IMLEDGTLLI
SIKNVKCTSL IRLKKQSIKY PSQNVYSHHW QSKDSPLTLI ENQLIEEKSS ESKINFEKLL
NDKLFNDYLI RLLNQSIKSE FIEFDYKTST VDTLEIDSNN TKLLEKIQSI LKTIDSLDQS
IDLASLKQVI IEKSSSFKKE INLIEKSIKR IVSLLKGGES EHFSPSNPSS PNDTPRYNSN
NCSSKSNNTS SGADDDTNNE ETINQLNNEP FNFSNSQFIS NQNQLISKTI VNSFDRLINS
IEIGEKKLIK IIDLSSIYQN NQLSKLLLLQ LNQLLINLSN NNNIEIEYTI PSNTKNIDSI
KEETKSISNL LNIKYRSFDL QDDLESNGYL NSNYDLIITS LLLVSTNSID SNEVLSKLYK
LLLPKGQLIL MEPPKDVLSF NLLFANDFKQ SLEIKSEQEI KSLIRYCGFT KIETNNITQD
DEEEQQQPPS ILIVQTEKRD IESMSLTFSS DPESLNSSYS NCIFIVSKEQ KENPTSYIQE
YFDITEVFCD NTTIIEAGDS ELLTKTIESG IGKNDIIFFL VSLEELTIEN YKQVTMQYTL
VNQILLRNNL STRFALLTYD SQNGGKNYLG SSLIGTFRYF LEFPSLNTFS IDVDKDSIDN
LTLFLRLVDL STIGDRETIV RNNKIFVQKI FKEPKLLSPS NNYEKDTNNL YLNTNSNLDF
SFQCKEKLPH GSVEIKVMST GINYKDNLFY RGLLPQEIFT KGDIYSPPFG LECAGYITRV
APSGVTRFKV GDQVVGFASH SLSSLAITHQ DKIVLKPENI SFNEAAAVCV VYATSYYSIF
HIGAFMADKE SILVHSATGG VGLATLNLLK WKRNQLKKHG NSEISNDASI YATVGSKEKV
DYLQEKYGDL ITAIYNSRDT EYCDEIKQQS AQGGVDLILN TLSGDYLSAN FRSLSQVGRI
MDLSVTQLVE NDSLDFSNFK YHVTYSTIDL ERATTYNSKI VRDILTEVFD AISDGSLENI
PVKVFPATQV KTAIEYINER VHIGKIVVDF ENFEQDILKP ALQEKENPIQ LNKVKKLEHT
CDTLNNTILI TGQTGIAVHI LKWIISGSVL NSNKSQQQVT DFIILSRSSL KWELENLINQ
TKHKYGDRFR FHYKSVNIAD LNSTRTAIDQ VYSSCKNVSP IKSVLHFATV YEYILPEDIT
QTVIDNTHNP KAVGAINLHN LSIEKDWKLE NFILFSSIGA IIGGSKQCAY SSANLVLDSL
SNYRKSIGLA STSINWGGLD AGGVAATDKS VASFLEGQGI LLVSLSKILG CLDSVFQPSN
SHLSNFMLSS FNIDNLLSSA PQMKRKMGHH LTNYKTSSAS SDDSLGDSSS TQAKVISTIS
ELLSIHPSKL NLDTRLKDYG IDSLLTVQLK NWIDKEFTKN LFTHLQLSSS SINSIIQRIS
SKSTSTSTPN PTNTTKQTAT TKT
//
