ID A0A495X852_9PSEU Unreviewed; 3515 AA.
AC A0A495X852;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Type I polyketide synthase PikAII {ECO:0000313|EMBL:RKT70182.1};
GN ORFNames=DFJ66_3431 {ECO:0000313|EMBL:RKT70182.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT70182.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT70182.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT70182.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKT70182.1}.
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DR EMBL; RBXR01000001; RKT70182.1; -; Genomic_DNA.
DR Proteomes; UP000272729; Unassembled WGS sequence.
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: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; cd05195; enoyl_red; 1.
DR CDD; cd08952; KR_1_SDR_x; 1.
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; 3.40.50.11460; -; 1.
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; 3.90.180.10; 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 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-like_N.
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; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR036299; Polyketide_synth_docking_sf.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
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; 2.
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; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
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.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000272729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..443
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1326..1401
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1413..1836
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3356..3431
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3515 AA; 369419 MW; A9A7724A73203136 CRC64;
MANEDKLRDY LKRVTVDLQK TRQRLHDVEA AAHEPIAIVG MACRYPGGVT GPEDLWRLVA
SGTDATGAFP TDRGWDLAAL HDPESQREDT SYTARGGFLY DAADFDPAFF GISPREAVRL
DPQQRLLLEV AWESLERAGI DPASLAGSPT GVFTGLMYHD YAGSNSSGSV VSGRVAYTLG
LEGPAVTVDT ACSSSLVALH LAIQALRRGD CTLALAGGVS VMATPLTFVE FSRQRGLSPD
GRCRSYSADA DGTGFAEGVG VLLVEKLSDA LANGHHVLAV VRGSAVNQDG ASNGLTAPNG
PSQQRVIEAA LVDAGLSTNQ VDVVEGHGTG TTLGDPIEAQ ALLATYGQDR SDPLWLGSVK
SNIGHTQAAA GVAGIIKVVE AIRHGVMPAT LHAEQPSDQV DWTAGNVKLL TSATPWPETG
RPRRAAVSSF GFSGTNAHVI IEQAPDQEVP GTASAPVTSL LVTARDPRAL RDQARRLASV
VSTVDPAELG YALATSRTRF EHRAAVVGTS AAELADGLAA LARDEKAAGV VQGRVAEGKP
AMLFSGQGAQ RLGMGLGLCE AFPAFAAAFE EVCAALDPHL DRPLRSVLET EELHQTGYTQ
PALFAIEVAL FRLLESWGVT PSALVGHSIG ELAAAHVAGV FSLADAARLV VARGRLMQAL
PSGGAMLAVE ATEDEVRPLL GADVDIAAVN GPRSVVVSGA EDAVAAVEAH FADRRTKRLT
VSHAFHSPLM EPMLAEFRAV AQSIAYRESA LPILSTVDSA GDFTDPEYWV RQVRATVRFS
DAVRAVEAKT LLEIGPDAVL ATMAADSVAD DVVLIPLLRK DRDEPRALVE ALARLEVRGV
TVDAEAFYGR TGRSLVELPT YAFQHERFWM DSVQAFTAAG PGDPLRYEAK WERLPSGTAR
TLTGTWLVVG PESAEVAGAL AANGATTVTA GLDGVAESLA EVAGVVSLLG AADTLKLIKT
VAPQGVPVWA VTRGAVGTSP ADPVTDPDQA LVWGLGRVAA LELPQVWGGL VDLPAVLDDR
TAAALATVLA GIGEDQVAVR PDGVFARRLH RAPAGPARRQ SVTGTVLVTG GTGTLGIEVA
KAYADDGADH VVLLSRRGTA PAEALAGIDA RVTVVACDVA DRAALEAVAA QHDDIHAVVH
VAGLAQLTPI ADMTDAEFAD VVSAKVEGAR NLDAVFPDVA EFVLFSSVAG VWGSGAQGAY
AAANAYLDAL AAQRRARGKA ATSLAWGPWA GSNLVDDDID AALRKRGLSP MAPDRAVAAM
RTALAAADTA VVLADVDWTA FVPSFTALRP SRLFDAIPEA VTETDTGSTD DLARLLADVP
EADHLDHVTT LVRTQVALTL GYAGPEAVEA TRAFKELGFD SVTAVEFRNR MIEVTGIRLS
AAVAFDYPTP QALAEHLLAS GTHEVVSATG FSDEPIAIVG MSCRFPGGVA TPEQLWAMLR
EGRDGIGPFP ADRGWDLDGL FHPDPEHPGT SYVREGGFLH DLPGFDAAFF GISPREAEAM
DPQQRLVLEA AWTAFEDAGI DPTSLRGTPT GVFVGTNNND YIRLTGAVGA SAEGFMATGN
AASILSGRLS YVLGLEGPAV TVDTACSSSL VALHLAVQGL RSGECSAAVA AGVTAMSTPG
AFVEFSKMRG LAPDGRCKAF AAGADGTNWG EGVGVVVLMR LSDAVAAGHD VLAVIRGTAV
NQDGASNGLT APNGPSQQRV IRAALANAGL EPSDVDVVEA HGTGTALGDP IEVDALFATY
GQDRDRPLWL GSVKSNIGHT QAAAGVAGVI KTVLALKHGE LPKTLHVEEP TGHVDWSGGV
RLLADAQPWP RGERPRRAGV SSFGFSGTNA HVIIEEPAEA PAPERPASPE PVALVLSARS
QAALQQQAAD LLPLLDTEEP RDLAYSLSLR AHHARRAVVA GDLRAGLTAL AAGEPSPSVV
TGTANPAGKV AFTFPGQGSQ WAGMAVELLD SSPVFAQRMA ECAEAIDRFT DWSLLDVVRA
VEGAPSLDRV DVVQPVLFAV MVSLAALWRS HGVEPSAVIG HSQGEIAAAA VAGALSLEDA
AKVVTLRSNA LLRLSGKGGM VSVPLPADQV RERIEHFAGR VTVATVNGPR STVVAGEPEA
LEQLLAECAD NGVRAKKIDV DYASHSAYVE EIHDELLDVL QGLAPRTSDV PFYSTVDSCW
LDTTLMDAEY WYRNLRQTVW FQPAVRALLD AGFTAFVESS PHPVLTIGVQ DIIDDAEATA
SVVGSLRRDE GGLARFQLSV GEAHTHGVKV RWPHGDARKV RLPGYPFQHE RFWPEAGAVV
ADAAGLGLSA ADHPLLGAAV AVADTDGLLF TGRLSVGTHP WLADHAVGGQ VLVPGTAFVE
LAVRAGDEVG LGKVEELTLT APLVLPEKGA VQVQMWVGAP DETGQRPLKI HSRPNDDTPW
TRHAVGLLGE ADQPTTFEPV WPPEAEELPV ADLYDTLATA GLHYGPSFRG VRRAWRRDDE
ILAEVGLPEP AGKAAFGLHP ALLDAALHPL ALSTTSQGPL LPFAWTGVSL HAAGATTLRV
RLRPTGQNAV ELTATDHTGT PVATVESLVL REAAAPTTQT THHDALFRLD WTPLTTSTDL
SYPGGTLETG AGGHRWATLG TLDLPRKAGL VTDTYATLAD LKTALDNGAP VPDRVALPCF
QTAQDPVQGA YQAVTTTLET LREWLADERL TESKLVVVTR NAISTHDPAE DLAHSPIWGL
VRSAQTENPD RFVLLDIDDR DPHRALTTTE PQLAIRDGVA YVPRLARATT TPALVPDTDR
WRLDVTEKGT LDNFALLPAG DPKPLGPGQV RIAMRAAGLN FRDVLIALDM YPGDGVMGGE
GAGVVVETAP DVEGITPGDH VMGLFHDAFA PEVVTDARMV VRVPKGWSFA TAAATPIAFC
TAYFALVDLA EVKPGEKVLI HAAAGGVGMA AVRLARHLGA EVFATASPGK WDALRGMDLD
DDHIANSRTL DFEDKFHGID VVVDSLAKEF VDASLRLLRP GGRFIEMGKT DVRDPDKVAQ
DHRGVAYQAF DLLAIDPDRV AAILRDVLAL FEDDKITPLP IKPYDLRRAP EAFRFMSKAK
HVGKLVLTVP PRRDPDGTVL ITGGTGTLGG LLAKHLVTDH GVKHLLLTSR RGLQAEGAAD
LAAELTALGA QVTIAAADAA DRGQLAEALA LVAPEHPLTS VIHTAGVLDD GVVTALTEDQ
VRNVLRPKVD AVVNLHELTH DLAEFTVFSA AAGTLGGPGQ GNYAAANVFL DTLVAQRRAA
GLPAQALAWG LWGEASGMTA HLDANDRARM ARGGLLELSV AQGMALYDAA QRIDEPLLVP
MPVDPTALRE LSRVDMLPVL LRGLVRGPAR RTLEATQSAG AFKDELLRQS GPQRRHTALE
LVKAQAATVL GHSSANAVEP NKPFTELGFD SLTAVEFRNR LKAATGLKLP ATMVFDYPTA
AALTDFLLAE LAPAEVDPAE ALLGELDVLE RSLAGADVDE SVKARITERL QAVLSNWRGQ
SDAGADAGGP DVDTVLKTAS ADELLRFIDD ELGAA
//