PKS28_DICDI
ID PKS28_DICDI Reviewed; 2690 AA.
AC B0G170;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable polyketide synthase 28;
DE Short=dipks28;
DE EC=2.3.1.-;
GN Name=pks28; ORFNames=DDB_G0290469;
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 pks27/pks28 in chromosome 5.
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; AAFI02000163; EDR41037.1; -; Genomic_DNA.
DR RefSeq; XP_001733033.1; XM_001732981.1.
DR AlphaFoldDB; B0G170; -.
DR SMR; B0G170; -.
DR STRING; 44689.DDB0235222; -.
DR PaxDb; B0G170; -.
DR PRIDE; B0G170; -.
DR EnsemblProtists; EDR41037; EDR41037; DDB_G0290469.
DR GeneID; 8627661; -.
DR KEGG; ddi:DDB_G0290469; -.
DR dictyBase; DDB_G0290469; pks28.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; B0G170; -.
DR OMA; RNWIGAY; -.
DR PhylomeDB; B0G170; -.
DR PRO; PR:B0G170; -.
DR Proteomes; UP000002195; Chromosome 5.
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; 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; 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..2690
FT /note="Probable polyketide synthase 28"
FT /id="PRO_0000369419"
FT DOMAIN 2594..2671
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 168..221
FT /note="Beta-ketoacyl synthase"
FT REGION 651..684
FT /note="Acyl/malonyl transferases"
FT REGION 916..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 906..934
FT /evidence="ECO:0000255"
FT ACT_SITE 187
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 661
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2631
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2690 AA; 305894 MW; 938E7F10BAD7C5CA CRC64;
MEKYDIYYNS NEEYYGDVAV IGIGLRFPSG DLNESISKPN QLFNSLLNGL NGIVTTSERW
SDNYYLNGEI NSVSAGLLPL DEWKRFDPIF FGINPSYDNV VTIDPQQRLL LKCVWEALED
SGIDPISLRG TNTSTFIGSS TTDYGSLQKS PFETQNNIFG SSNHSVANRI GYNFDFRGEN
FTIDSACSSS LNAINCGYNS IKSNKSNVSV VGGVNFILDP HVSKSFTQLN MLSPTGKCHS
FSSDADGFVR SEGVGIVILK KLKDAIKDSN NIYCVIKGSS SNVDGNYDKL NFYSPSKSSQ
YENMKLAIKS TNGQINESDI DYCEAHGTGT PTGDPIELEG ISRLFDQNNN NKKQVLVGSI
KSNIGHTEAC SGVASLIKCC IMFKNKLFLQ NINFKESNPL INFKEWALKV VTEPITFNEN
KTTVMLINNF GVTGSNVCLI LSEFKDKRYS NDESSSDNFC EQIDIDSKAN EKKKFLIPLS
SNSSTSLDNY KSIIVNNNDD DSNSSTRSFQ EFVYNQIKFK STSLIQKSVI IASDWNEFQD
DDNQIKLKNS ESLISNITVE KKKSPLTVIV FCGQGSQYNR MALSLYENEP IFRESVNRFD
KELFKYYGYS VLDRLRSVSD KDEISIHLPI LAQPANIMIQ ISLYELYKHW GVSADIIVGH
SLGELSSSYS SGMIDFETLC HLIYHRSLAQ NKTTGTGRAL SVNISYDEFI ERYQSKNNKY
ETLEIACYNS PTSIVIAGKE DLLNEISKEF KSNDIFCAML GSLSSFHTSS QLMIKDEVCS
LVFKSKLPSV PVFSTVTTNL FNDQTPYNAN YVWENIRQPV SFTQTISNLY KHIESNDMGN
EITFIEVAPH PTLQFYLNQM KSTQSSYFNN GKSVTIYSPL HKKKNDYNEF LKTISLLYVN
NNFNINFKSQ LTNINNNNNN INNNNNNNNN NNNNNNNNNN NNNNNNKIIQ FNINSLPLYQ
WDDNEYFKLN PFHEKITNEG PSIQNLGNGI DSACPTYQTF IDIKKPPFQW LKGHQVSDKF
YYPGMGYVQN LLSIYPNQDI TISSLEFKSP LVLTEGNNQC LETTVSLLSK NEFNVKSHYK
DQKTNQWILS SLGNFSLFKH NSINSEKLIN IQALKDKCNF TTISKHDFYE SIKIKTNLTY
KGLFQGVKEC SIGNNCSLAV VSLNEINNHT ISNHSTIGRS LFNAATLDSC LHGSLIAVAQ
PVVLDRIEGF KLYSSNIPLS SSLSKDDNDN SNNSLIKELY IFTEEKARTN YQSFSASVKI
ILPNGRLLME ISRVVCSSVS LANPSNTIIC KPPSNEIYTP YLQPKDSIIN KPQQFKHLYS
VDEFIAKEED NQIISTELLL SLFYKHINVR CPTINLESLT TLEYNQFKQL YYNNNGLVNE
NLFKFVFEIL KSYSSSNHYI LNHHNNSENK NKNNNNNNNS NNNENSNNES PIHFEKLYNL
YTKTTKIIAK QIFPLKDDSF TDTPQSLFEN GFLDDFYKNS RVVQPLNNLL SEIIIEALKP
ILNQPIVFRI LEAGGGTGSL SLLILEKICK LLNANPNSVI DIEFTWSDVS SSFSAEIKEK
FSPFTAHKNF NIIHRVLDLE KPLFDQDFKT SYYDLVVMSN VMHVVKKLKP TLDEIHNILT
PNGQLLFVEP PYKSINYDSV FCCFSQWWPS SDSDTELRPD RSCMNQDKWI KILNETNYRD
TIISGNDNLI FLIQTRKPSI NEIISKQSSD SSLDQFNSFN NIILFGNNNY GCSLQNSISS
NQELKSKTIN INNFNEFQTW IANNYDNSDD FDNNKTLIIF LKSIEPINIS NFKEITYEYI
QINQLILKLE LTNNFKHLLI SLDSTTDNYL SSSIIGAARY FVEYPQLDLY ILNYDIISLK
ILNNNSSSSC NSSNGSISSC SCKQQQLSLI NYLINTNNNI QKEFTINNNK VYYERYTRHS
NKIKCNLQSK SFETNKDNLL IQLDSNLEYQ LYSKRVEPNS KEVEIEIKAT GINYKDYLMH
IGMVSSDLDL KYGKEYEVEN CIGIENPMIG NDFSGIITRL GSDAEKKKFK VGDHVCGVAS
KTSGSHVVID YNFIYHQPLN YNHSISASIP SIYVTSLHSI YGVGNLKSNE SILIHSAAGG
IGISSLDLLK CKKHQGHIFL TVGSKDKEDY LKKNYGSFIT AIYSSRNKDY VNEIKNKLIE
LGEVKQQGVD LILNTLSSEF MDSNFQCLNM SGRIVDLSVT HLTPNDYIAN NHFKYNMGYN
NVEMIDFNGK MVRSYLKKII KMINSNKLEL SIPIIEYSNN QFKDAIEYIN QRKHIGKIIV
NHNQDEFNRV YNNYQQNNNN NNQIIMKHSY DISKLNMGKN ILLTGQTGII LEIMKYLIRY
SNHSIQNIII LSKSKLKWEL ELLINQTKFI KDNIIKFHFI QIDIEDSNKV NQVLNQLELN
ENITNIDSII HFAFNNDIGD VQDVNMNRLN IAHGAKTIGA INLHNESINR SWKIKQFIIA
SSVSSIFGSD QQCCYVSACS VIDSLSKYRH SLGLPSLAIN LGTVASTGFI SRNNAIETMF
KSSFLKLFSP QLVISSLDLF IQNQRQYPNY SLVDFNFEVM LTSPNYHLYK LDYEINIFKK
SYQINTNSSS GSGSDNEFIH STILNKISEL LSIDESKINE DLQLTQYGMD SLVIVQLKNF
IDNQLGHNLI TIHQLQHNKI NQSIDIIKFG YLINKNKFKY KNNNKNNNNG