PKS14_DICDI
ID PKS14_DICDI Reviewed; 2998 AA.
AC Q558Y6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable polyketide synthase 14;
DE Short=dipks14;
DE EC=2.3.1.-;
GN Name=pks14; ORFNames=DDB_G0272859;
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=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).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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.
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DR EMBL; AAFI02000008; EAL71067.2; -; Genomic_DNA.
DR RefSeq; XP_644930.2; XM_639838.2.
DR SMR; Q558Y6; -.
DR STRING; 44689.DDB0235176; -.
DR PaxDb; Q558Y6; -.
DR PRIDE; Q558Y6; -.
DR EnsemblProtists; EAL71067; EAL71067; DDB_G0272859.
DR GeneID; 8618609; -.
DR KEGG; ddi:DDB_G0272859; -.
DR dictyBase; DDB_G0272859; pks14.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q558Y6; -.
DR OMA; DEWIECA; -.
DR PhylomeDB; Q558Y6; -.
DR PRO; PR:Q558Y6; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 CDD; cd05235; SDR_e1; 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; IPR013120; Far_NAD-bd.
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; IPR010080; Thioester_reductase-like_dom.
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; PF07993; NAD_binding_4; 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; 3.
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 Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..2998
FT /note="Probable polyketide synthase 14"
FT /id="PRO_0000376887"
FT TRANSMEM 1979..1999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2621..2641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2476..2553
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 170..223
FT /note="Beta-ketoacyl synthase"
FT REGION 657..690
FT /note="Acyl/malonyl transferase"
FT REGION 2559..2578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2559..2575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 667
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2513
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2998 AA; 340936 MW; 1E24DFBA0F03FD91 CRC64;
MTNNTNLSSY KLAKPNENED DIAIIGIGFR LPSGDLSKSN DSTKELWNNL MNGFDGVVKT
TERWSDNFNE LGEISNGNAG LLPLDEWKSF DPLFFGINPS EVSTIDPQQR LLLKCTWEAL
EDSNIDPIKI RGSKTSVFIG CTSVDYKDIS KNPNSTQTNV FGSALSTIAN RISHCFDFSG
ESITIDTACS SSLNAIRLGY QSIKSGFSNL SIVGGVNSLF ETNSSKSFSY LNMLSKSQGK
CMTFDESADG FVRGEGVALL VLKSLKQSVA DGNNIYCVIK GASSNVDGNG LKDKQNFYSP
SSISQADNVN NAFSSTNGTV KLEDIVYIEA HGTGTPTGDP VELDGMSRVF KTHSSNNSTL
SQQPLLIGSI KSSIGHLEAA SGSASLVKCC LMFKNKYLTP NINFKNPNPS IKFDEWNLKV
VTEPIHFKDL QKTDNFSMIL NNFGITGSNC CLILSEYKGN NKNNNNKNSC THSEDLKNLQ
TQKQYLVPFS ANSVQSLKQY ESVVNDYLFK KSNDFKEFVK QQIFSKSSSL YQRCVVTASN
WNEFSENIES TNKIQTSNTQ SSNMSKVQNN PITVFVFAGQ GSQYNTMSLE LYNNEPIFKK
SMDLLDDELL KYYEYSVLNK FRSIIDDGDR SIQHPTIAQP IVCMLTISLF ELYKHWGIEA
SFIVGHSLGE IPAAYCSGMI TLDTLCYLIY HRSLAQIETH CNGGRMLSIG ISSEDYLSSN
YSTKYPDIEI ACYNSPNSIV LGGNEQQLNQ ISNELKDKGI FSTMLASLSS FHTSNQKITK
DQILNLNINH QSPTIPIFST VTTNLYESST TPFNSEYVYN NIIKPVKFSQ TISNLYKHIE
INKLGNEIVF IELAPHPTLQ FYLKQMIPVS SLSTTEETNF KVSIYSALHK KKNDIQEIQK
TIAKLYCDNR YNINFKSQFK DEQIINNNNN QEIILPNYQW DDKKYWKEDL VQQKHKFQGP
PIDQLGFSLI ESSPNVKSYQ TFIDISKKPF KYLKGHIVNG KYYFPGCGYI DNLLKLYPSQ
DLTIGSMEFK SPLILIDGIN QCLQTNIFQT GKTEFKVQFH FKDNKSNEWV QSSNGNFQLF
TSGNNVNKKY NIQELINNKC NLTKLTKNEL YQNIKSKTGL SYNGEFQTVS ECYLGDDCSL
AVIPIKPSSS TLFTPSVLDS CLHSSVGLVD EQCQLVFEKV EGFKYYSSNI PSFLELSSDK
EIKLYSYSYS FKRIGDSFSS SIIVMFEDGR ILIEMNKLVC KSLTIIKDSS IIQPPLNDLY
STYNQLIDSP IPSPSKFTQQ LDEPDRMNEK VKNYDISILK NFISNQLYSN IVKRCPQLNI
EIIKSMDIIQ LLEKYLNDDK HSKLFKSIFE TLKDSVIDVN NVDDHQHYYN ENNIEHYEIL
LKSTKIVAKL LFPLIDDDPS NDTPQSLFDN GMLDNFYSNY HILKIHNQVI ANIISESILP
NLNEKMVFRI LEFGGGVASL SLIVLNKINE LLIEFPNSEI DIEYTWSDIS PSFIPDAKSK
FSHINQNIHI IYKPLNLEKQ LITEQMLKPS YYDFVIMSNV LHVVKQLKPP INQIYEILKP
NGQLVFVEPI YKSILLDNIF GVFDQWWCFT DLTIRKDRCC MPKESWNNLL LDCSFNEVKV
IMSIEIPSFY VIHTQKPSIY SNLNNIETIT QINDDNNNNI IIYGDNELSL FKEVSTTTIS
NVQQFNELIK KSIITDKSIV YFTKAINQLT IDNFKFVTLE YIQINQILLS NNLKCKNVLI
TLNSDNINYL SASVIGAARY FEVFPQLNLF SLDFDQKSIN NKELNNTIQL LLDSNKFIQK
EFKIRDNKVY YERYKRNSNL NKTFVISESF VNDINQLYAK LSPNLEFILD SKKSLKENQL
EVHVKATGIN YKDYLLYCGL LPPEMVSHNN DINDPEFGLE FSGIVSAIGS NINDFKIGDQ
IYGIGYDTTS THIIVDYNQI YHKPTNINHI EAASIPGVYL TSYHSIFNVG NLKIKRNESI
LIHSGSGGIG LSALNILKWK GHKSHIFVTV GSKEKEQYLI NTYGDFITGI YSTMNKDYSE
EIKLKLKQLK SDKHGVDLIL NTLSSDYMDS NFKCLNIGGR IVDLSITHLN PNEYINNNNF
KYNFGYHNVE LLFIEKTLIQ RMLKKITRAI ENHELNLMPI TEFSNSTIKV AIEYINKRKH
IGKIVVNNDI NILSDLIDVH KNQINSNFSI LKTNYKINSN NQDHLGSTIL VTGQSGIILE
ILKWIVKFSE NVKNIIVLSK SSMKWGLELL IKKNKHINFH FKSVDVSNSI SVDNAIDQIL
NGNSKTITNI DSIFHFAFEF TFCGVNEIDM KSLEISHGAK TMGAINLHNQ SIKRNWKLKQ
FILSSSVASI IGSVDQCSYV CSNRVLDSLS RYRKSIGLPS ICTNYGSVQS AGLVSRNESI
AQLLDGQGLY PLPINMILGL LDSQIQNVFQ STNLIVSPFN FKTLFEHYKK HPMIHKFDFI
TNLIENNELT NNKKIENDTS IDSLFLNKLS ELLSIEVSKI NQDLRLLEYG ADSLLTVQLK
NWIDKEIYSS LITIQQLQSN TISSSIKLIT NQLKLKIGDG QQQQHRQNKK NNNIPENKTI
ESEEFWKNEI KLDDDEFNLI SSNSIRNQIE IKEFKENELR IFLTGSTGFL GAYLLWYLIQ
MECCSVVYCL LRNKSKSSNP VDEILNNLKH HQLYYKQLNE KHLSKIIPIV GDLTKKKFGL
SDYNYSLISN NTNLLLNSGA DINLRANYYE CKQVNVNSLK EIIKLSLFGK PTQQQHHQPK
PILTISTFSV FYNQEFNGSI ATPKLETINN LPTGYMQSKV ISEFLLTEAS SRFKIPSIIF
RAPSIFSNPD TGIGHYGDIT QLMLQSSFKL GYFPSDKEVD INLLCSPVNW VADNIIKIMF
NDNFKDSSDS SLKIYNVYGE VINSVKILQV LKNEKGGNCK EVNFKQWKRM VMDSNEKVCI
KLRTFHTLDF DQKYNFEKAY GISKEQISFL QSIGSYGNGG ENNLIQMIFN HILAKYSK
