ID G8SJL5_ACTS5 Unreviewed; 2753 AA.
AC G8SJL5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:AEV86942.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:AEV86942.1};
GN Name=pks1A {ECO:0000313|EMBL:AEV86942.1};
GN OrderedLocusNames=ACPL_6055 {ECO:0000313|EMBL:AEV86942.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV86942.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003170; AEV86942.1; -; Genomic_DNA.
DR RefSeq; WP_014693012.1; NZ_LT827010.1.
DR STRING; 134676.ACPL_6055; -.
DR KEGG; ase:ACPL_6055; -.
DR PATRIC; fig|134676.3.peg.5946; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_8_11; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AEV86942.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEV86942.1}.
FT DOMAIN 35..447
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1628..1703
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1722..2134
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2611..2686
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2753 AA; 284620 MW; 9BC94ED087089B3A CRC64;
MGDEEKLLTY LRKATAELRD ARQRITELES AGTADDPVAI VAMACRYPGG VTSPEDLADL
VLDGRDAVAG FPDDRGWNVE GVYHPEPGEP GRTYTRQGAF LHDAAWFDAG FFGIGPNEAL
LMDPQQRLLL EISWEAFERA GIDPRSVRGS ATGVFTGMMY HDYPEAHSTG SVASGRVSYV
FGLEGPCVTV DTACSSSLVA VHQAVQSLRT GECRLALAGG VAVMATMDTF IEFSKQRALS
ADGRCKPFAA AADGTGWGEG AGVLLLERLS DARRNGHPVL AVIRGVATNQ DGASSGLTAP
NGPSQQRLIA AALADAGLTA ADVDAVEGHG TGTVLGDPIE AQALLATYGA DRPADRPLWL
GSLKSNIGHT QSAAAVGGII KMVMAMRRGV LPRTLHVDAP SPKVDWSAGR VELLTEARPW
PAGERRRRAG VSSFGVSGTN AHVILEDVAD EPAPDDTAPA PGIVAWPLSA ASADGLRGQA
ARLAERLPDA TPAAIGHALA TGRAALSHRA VVVGADLPEL LSGLAEVAAG EHEAGVSHDR
PAVVFTFPGQ GAQWDGMAVE LIETAPAFAA ALERCADALA EFVDWNLLDV LRGVPGAPTF
DRVDVVQPVL WAVMVSLAEL WREHGVEPAA VLGHSQGEIA AACVAGALSL ADGARVVALR
SRVIATGLAG KGGMLSVPLS RAVAEQRIER FAGRLGLAAV NGPGSVVVCG EPTALDDLVA
ELTEAGLQPK RIKVDYASHS HYVAEIEAEV RAALAPVRPR PASVPFYSAV TGGLLADTTV
LDAGYWYRNL RQTVQFEDAT RALLDDGHAL FVECSAHPVL QVGLQDTIAD AGAPAGTVES
LRRQDGGLRR FAGSLAAAWA RGATVDWARF SPAARPADLP TYAFQRERYW MAPVAGADPV
SLGQQPLRHP LLGAAVPLPG TDGLVATGRV SLTSHAWLAD HDALGAVLLP GTAFVELAIN
AGAQVGCGVL AELTVQAPLV LPDRGPVALQ VLVGGPDEDG ARPVAVHARA EGGDAPWVCH
AAGLLTPDDG GPAPGHPDDS WPPAGAVAVD VTGAYDGLLG RGYAYGPVFQ GLRALWRRGD
EVYAEVALPE PAHADAALFG LHPAALDAAL HAALLTSDPD GTVLPFAWTG VRLHATGATE
LRVRLAPAGT GSSIHLTDPA GRPVLSADGL VSRPVSAEQL AAPGAPRDVP YRLDWMPMPA
AGTAPPVRWR EVGGLDELTG DDDLPDVVLL RAPAADPADL PAALRETGAA TLATLRRWLS
EPALDGRRLA LLVEPDTLLG DTVRGMLRAA QAEHPDTFLV LDHDGRPESL AALPDALAAG
EPEVSIRSGR PHLPRLVAAG PPDAAARPDP AGTVLVTGGT GGLGALVARQ LTTDCGVRHL
LLTSRRGPAA PGAEELVAEL TERGVQVTVA ACDAGDRAAL AAVLAAVPAE HPLTGVVHAA
GVLDDGLIAA QTPERLDAVL RAKADGAWHL HELTADADLA MFVLFSSVAA TLGGPGQTTY
AAANGFLDAL AAHRRAAGLP ATAMAWGLWT GAGMGDRLRE ADVRRMAADG LPPLPVADGL
TLFAAALRTD AGHQALLRLD PVVLRAQAAA GELHPKLRAL IRVPARRAAG ETSLPRRLAG
LGRPERLALL ADEVRRRAAA VLGFTDPAGV DPGRAFRELG FDSLASLQLR NALNALTGLR
LPATLVFDHP SCAAVAGHLD ELLMGAATAD DRAGDRVATA DGEPIAIVGI GCRFPGGARG
PAGLWRIVDE GADVIAGLPA DRGWDLDNGY HPEPGTPGRH YARGGGYLHD AAEFDAEFFG
ISPAEALTMD PQQRLLLEVS WEALEHAGID PATLAGTDTG VFAGLMYHDY PLNTATGSIA
SGRLAYTYGF EGPAVTVDTA CSSSLVAVHL AVQALRRGEC GLALAGGATV MSTTETLVDF
SMQAGLSPDG RCRSFAAGAD GTGFAEGAGL LVLERLADAR RHGHPVLALI SGTAINQDGA
SNGLTAPNGL AQQRVIRAAL ADARLTAADV DVVEAHGTGT VLGDPIEANA LLATYGRDRP
ADRPVRLGSI KSNIGHAQAA AGVAGVIKMV EALRHDTLPR TLHAVQPSPH VDWDAGAMRL
LTEPAAWPGG DRPRRAAVSS FGISGTNAHL ILTEPPAAAP AEAPVAAGAP VVPWLLSARS
PQALREHAAG IARVAAGLRP ADVAATLARR AALPHRAVLA VADPAEGIAA LTALAAGDPA
APPVETAATA TGCVFLFTGQ GAQRLGMGRG LYERFPVFAG AFDEVLAGLV PGLRDVMWGG
DAAALDRTGH AQGALFAVEV ALFRLVESWG VVPAAVAGHS IGEVAAAHVA GVLSLSDACA
LVVARSRLMQ ALPVGGAMTV VEASEAEIGP YLGRVDLAAV NGLTSVVVSG AADAVAEVAA
VFAGRGRRTR ALRVSHAFHS AHMDPMLDDL RDVAAGLEAA APRIPLLSTL TGRWATAEDI
TTAGYWARQV REPVRFHDAV VALAATGARV ALELGPDAVL AGLGPHCVPD SDLDFLPTLR
RDRDEERALV TAVTAAHARG VPMDRAALLA GTGGVPVDLP TYPFQRRTYW LTAGDSSGIA
ALAGAVDSGD DAFDAGLPAM IAGQSPAQRH LTLVDMVRVH AAAVLGHPDV AAVPIDRPLQ
ELGFDSMAAV SLRRRLTAAT GLTLPSTLAF DHPTCEAAAR FLATRLAEER EPDEALATVV
RLETLLADTT PTAEVTARLE ALLRTWNDRA ATGGDGLSDE ELFARLDREY GGV
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