PKS45_DICDI
ID PKS45_DICDI Reviewed; 3092 AA.
AC Q54B49;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable polyketide synthase 45;
DE Short=dipks45;
DE EC=2.3.1.-;
GN Name=pks45; ORFNames=DDB_G0293912;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-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 and clustered as a pair pks44/pks45 in chromosome 6.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL60455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAFI02000224; EAL60455.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_628867.1; XM_628865.1.
DR SMR; Q54B49; -.
DR STRING; 44689.DDB0230078; -.
DR PaxDb; Q54B49; -.
DR EnsemblProtists; EAL60455; EAL60455; DDB_G0293912.
DR GeneID; 8629483; -.
DR KEGG; ddi:DDB_G0293912; -.
DR dictyBase; DDB_G0293912; pks45.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; Q54B49; -.
DR PRO; PR:Q54B49; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd05235; SDR_e1; 1.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; 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; PF07993; NAD_binding_4; 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; 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; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Membrane; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..3092
FT /note="Probable polyketide synthase 45"
FT /id="PRO_0000371401"
FT TRANSMEM 2705..2725
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 2566..2644
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 151..204
FT /note="Beta-ketoacyl synthase"
FT REGION 640..673
FT /note="Acyl/malonyl transferase"
FT ACT_SITE 170
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 650
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2604
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3092 AA; 349205 MW; 37C3D134E8A7A60C CRC64;
MDSQNIKYGD NDVAIIGIGL RLPSSINRPS ELWEGFLAGF DGIVETTNRW SDSFASMDEI
SSKYADEWMS FDPLFFGIIP TEVPSIDPQQ RLLLKCTWEA FEDANIDPFK LRGTNTSVYV
GASSLDYASI NVDFDETPMN IFNSNMSGVS NRISYCFDFR GASLTIDTAC SSSLNAVHLG
YKSIISGESD YSIVGGCNFI MSPHTSRSFE SANVTSKTGK SKAFDQDANG FVRSEGVVSI
ILKKMSKAIQ DGDQIYSVIK GTNSNVDGNL NKGNFFAPSK QSQANNIKSA MESCNKETTN
STPIALNDID FFELHGTSTQ IGDPIECEGV SSVFKESREK PLLIGSIKAN IGHLEPASGV
ASLAKVALMF KHRQFVKNIN FDKPNPNIKF DEWKIKVCTE NTPFPNNKKV SIAINSFGIT
GSNVCLILTE YIKPTTTKTT NGTAILSTFP LLSTTTTATT NNNGNQKYLI PISANSKPSL
ESYKEKLINS SKEFSETINF KDFVKYQLDS KTLKLTQRSV IIASNWEEAG STQSIITTNS
NRSGNIIKDT NKNPQLVFVF SGQGPQWSKM FTQLYDQEPI FKQKTDQIDS LLSKHYGYSI
LNKLNSIKDD DTVTINEPIL AQPSVFMIQM ALIELYKHWG ILASISIGHS LGEVSSAVCS
GMIDLETGCF IIYHRSRLQQ QTSGSGKMLV ASLNEQKFNQ EFDNFQQKYP SIEIACFNSP
SSIVLAGKES ELQEISNILK EQETFSIFLG AQSSFHSSSQ EPIKDELLKQ LKDIKSTKSN
IPNFSTVTSN LFNDDDEVAQ QPDEASAHNT NTITLFDSKY VYENVRKPVQ FEKTIKNVFN
YIEKKGLGSS VIFLEISASP VLGNYIREMI PQDSNYFFIE DQTISVLSSL NKKNKDQVLE
IQTSISQLYC KGYNVNFNCS NQTNSLDFQN TEYKQLSDVL FKYSWDDESY WSVAPLISNY
IKNGPAINQL GNRNERQPYQ SYVSIIDIKK EPFEFFKGHS SRNRVIYPGC GYIDSILKAF
PDQDLTIQSM EFKSAVLLLP SMKTYLSTNI TPSGKNEYRV SFHYKDKKTN KWSLSCSGKF
SITKHNDEVV RKFDIEKLKA KTNFVTIQKK ELYETIKYKA QFTFEGKFQS IEEVSYGHNC
CLAKVPLTTL SSYDNQSFLN LCVIDSAFQP FCAVKENKEP MLFSSIENLK FFSKNIPKSA
EDREKHKFVY TYTQIKEKKC GSYFVSILTM LQDGTILFFS PLVVYTQLTP YKNQYIIESP
NDNLYKICYQ SKDSTLPSPL ILKDKFDQLN FETTDEQSQI IRKALSNCLF AIFKRNNNLF
TKEEIKSQSI DYLIEKYCLI IDNDDDNDGI DDNSILVNGG VASIDDMVLA STAGKETTIL
NNGKRVLAKL IFQILKSNVD LIDWDNIATF TNTSSKQQLN IIQAIDNLIV TPLSVTNQVT
ESDLISKTQL DIINNRMKIK QYELISNTIA TDLIKPIINN SILFRILEIN SGFGYLSEMI
INKINQLLIE FENSYEIEIE FTFTLNGTNQ DDNKEISNSI KEKLTNLLIS KSSISIIFKE
LNLNESFLEQ KFNPSYYDLI VLTNLSTITN LNESIEFINS ILYPNGHLII IDTKNQSNFQ
DYEIFEQFLI FDNFGGGIVD DNIDWNQIFQ NNNLNNAIVT PNIQPHVIQV QKSKLYDKVM
STLDDITGPY DQIIIIGDQM QDTNEDLFQN PIMDINKQGT DIYRIKTIEE FEKHCLTIPP
TDKSILFFIS AMNNLSLGDY KQVNFDYIKI NQYLLANKLR CPFILATRSA LKESTNALAA
SLIGSFRYFS EFSNILNLYS FDFGEMVFTI ASGSPFKWMN MAIDLLDPNK HIQREYIFRN
GNETWFERIG KIKRVKSKYQ SKSYLDDKED SLVARLNQNL EYQLEAKQSN LKENEIEVQV
VATGINFKDS LIFRNLVPPV LANHDGDYSK PEFGIECSGI VSRIGSKVTK FKVGDSVLGI
SWKSTSSHAI NYQDAFVLKP DNISFVEAAS IPLVYCTSFY SLFYSGNLKI ENNESVLIHQ
ASGGIGLACL NILKSCGFKS KLYVTVGSKE KEDYLRETYG DFITGIYSSR NTDFLENIKT
DLSKINNNNN EIKENNTINE SFDDVDQILP FIHKKGVDLI INTLPFEFLD TNFLLLGQGG
RIVDLSVNHL NNNDTTDFSK FKWFIGYSTV EIFYNGFEKS KHILQLIIDM IKNKELPLIP
IKEYPINQIK DAIEFIGQRK HIGKIVINHK VGLRDGCSNL VQDTIKSLQN HLKDNYLVAS
PDFKFMGDSL GKTILLTGQT GLSLSIIQIS LLNNYQDLEG IIVISKSPIR NELQYLISFA
KYLSRKTRVH FKQADCSKFD EISKAISEIY EKDDPNLSPV ESIFHNAFVP VMSEPQDIGM
KHIDDAYDAK TTGAMNLYLL AILNGWKLKN FFFSSSVASV SGSSRQAGYC GANLVLESIA
KTIQSQGIRC STICWGSIGD IGYVSRNESV SKYVHGLGNI SMPSNMVLGS LDLLLQQPTL
STDTTIVASF DFNNLPKLST NGSNNLYYKF DYFTNPIQSN QNNCSSDDLS IREEILAKFS
EFLSVDDQSK INLDIKLLDY GADSMVIVEL KNYLDKTYTP NILSIQQLQN VTINQLIQSV
TDAMNKLNGN ENKSIKKSNK LVQQKQIDWV KEIKLDSSIK PTDEMIKLFK QLQQQLASPT
TTTSNTVFLT GSSGFIGIYI LFYLIKSVNC KIVYCLIRRK TIEEATTFLI EFLKVHQLYN
QLTTDEINKI KPVLGDYTLD SFGLSVDQYT NLSNNVDLII NSAASVSFLM DYEDSKVESV
EGVLQCLRFS CHNKLKKFVQ VSTLGVYSDD KRDNLDDYTF AQIDPKIIQS KNSIINGYLQ
GKIVSEYHIK EAANRGIPCC IIRLPFIGPN PSTGVGNDSD FFQTLLQSCY AMSTYPKQES
GLQLYSTPVT WVAQNLSFIS MNPKCWSTSS NNPSSISENL TCYNLFGESI CFNVLLTELA
SQLKWKPTPP GEFLKKLKSF PNEPSCNKLH VVLKNSKNLL LNIYIPGNYK LNPTLKQLLQ
SNNTYKGWKI TPEMILTHLS FTFKKIKFIN YK
