ID F8TTL0_9BACT Unreviewed; 2546 AA.
AC F8TTL0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AEH26521.1};
OS uncultured Acidobacteria bacterium A11.
OC Bacteria; Acidobacteriota; environmental samples.
OX NCBI_TaxID=1036854 {ECO:0000313|EMBL:AEH26521.1};
RN [1] {ECO:0000313|EMBL:AEH26521.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21539584; DOI=10.1111/j.1574-6941.2011.01122.x;
RA Parsley L.C., Linneman J., Goode A.M., Becklund K., George I.,
RA Goodman R.M., Lopanik N.B., Liles M.R.;
RT "Polyketide synthase pathways identified from a metagenomic library are
RT derived from soil Acidobacteria.";
RL FEMS Microbiol. Ecol. 78:176-187(2011).
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DR EMBL; JF342591; AEH26521.1; -; Genomic_DNA.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013149; ADH-like_C.
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; 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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_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; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 26..454
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2463..2540
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2546 AA; 275973 MW; FD7F92914F9E9901 CRC64;
MLETAKPNCA GSSASPSLAP AIMPPGEPIA IVGIGCRFPG GVRHADSLWK LMCDGVDAIT
EIPKDRWSVE QFHHPDPLVL GTTYSKWGGF VEGMNLFDPG AFGISPREAV SMDPQQRLML
EVTLGAMEDG GFRPGALRGS SAGVFVGIST WDYSQLQYES SAGAKVDPYA ATGTALSIAA
NRISYCFDLH GPSMVVDTAC SSSLVAVHLA CGSIWKGECQ MAFAGGVNAF LSPANAIAFS
KMGVLSPDGR CKTFDTRADG FVRAEGAGVV LLKPLAQALR DADRIYAVVQ ATGVNQDGVT
NGLAVPNGNA QAALIRETLD RAGLDPGRVA YVEAHGTGTA VGDPTEAHAI GSTIGSRRNS
GPCLMGSVKT NIGHLEAAAG IAGLIKTALI MQHGAIPPNL HFQTPNPLID FARLGLEVPT
GLRRLHEENG AAAPLAMVNS FGFGGTNALA VLSAAPRKAA PAEPDGSGPW LIPISATSEE
RLGVLADSWS EFLGDKTNLE SIGRTAALRR EHKLHRLCLV AANGPEGAER IHSFRAGERA
PGVVTGKARS DSPPKVAFVF SGQGPQWFGM GRGLLAGNQL YRGKLEECDE LVRRLAGWSL
IEALSAPEEL SRIGETAIAQ PALCALQIAL AHVWMNRGIQ PVATVGHSVG ELAAAHVAGR
LTLEETMRIV VHRGDCIARF ARKGRMLAAA LHSDRAHQLL RDRGASSIAI AAFNGPGQVT
FAGATDALEV FAGCLEEDGV QHQLLHVDYA FHSDLMDPAR EPFLTAVGGT RSQAGAVRWF
STVTETFIDN GGIDGDYWWR NVRQPVRFVQ AVEQLIDEGC DCFLEISPHP VLLPSITESL
RARGREARVA FSLRRDADDE VSMLANLGQL HGWGCAVNWQ ALYPNPHPPV DLPPFPWMRE
SYWCAGEGGH RPWLEARVHP LLGTSASLHK PVWRTRIDLH RLPFLREHRL QNRALFPATG
YLEMAMAASR EILGVKRPVL ENLELRKAMF LPAEPETAEL LTEYEPADRE LRFFSRIGTS
TGGWTLHCRM RLGGDNGDAA APRFDRESAI RRCPETFPGE IIYEIGEVTQ LEYGESFRGL
KEFWRSSTEV VARIELPENV ELDEGGWIFH PAFLDACIQA GNLHKPLEQS AASVQGSTFV
PVGAGEMRLQ QKPTSRTLWV HVLKTRDTPR SQCGDIWIYD DEGFAVLSFR GFESQRLELK
AVGDGASIDD WTCELSFIPT PRPSPDAAQP APGRDGRWPS LASLAEEIRG SLEDILAGAA
RIKRFGVLRE KLNELALTWW ECAFRALGLA KCDGLAADIR GIIQACGIAP SQERYATYAV
ACLERAGVIR ATESKWTIAA EPVMRADPAT LWNEMLAEFP MAYAELMILQ TLGGNLPALL
KGETTLQEQL FNRAAEGLLD HFYQDSIGLI SRNAALAQVV GRLAAAPAGG RKMRVLEIGA
GTGGVTSHIL PLLEGRNVEY CFTDVSPAFL ATARRRYSDF NGVDYRVLDL EKDPVAQEFG
PHEYDVIIAA NVVHAVPDVA RSLAHIRRLL APDGVFCLLE VVTAPSSLHF IFGLTEQWWI
HQDDRMQPIS REQWQRHLAA EFSEVVDLSE GLDASGSELA EIAVFLARGD HIVSRSETTP
SAPDEIKTPD RAGNWLILGD RRLGPKLADL LSMKGASCLL VPAEAGLPRI AHELQVAIDV
GNPFDAVVHL WPLDCVSNDE LSLEAIERDA PLTWESALEL VKKIAQIESA SRPRIFAVTS
GIESVGGSVG PAALSQSTIR GVFTAAVCEY PALQMRLIDL DPAIPPGDQA GELLLELSSG
DTEQEVAFRD RSRFVARLRS ITLTETMDSG KIWLRHGTAH GEPGPRFELF VPSGGTLDRL
GYRETRERPL LRNQLEVRVI AAGLNFRDVL KALGRYPLDG DYLTLGDECS GVVERVGEDV
TEFRVGDEVI CAGAPCFASH VITLEHLTMP KPAHLMFEEA ATLPIAFLTA HYCLHDVAGL
QAGETVLIHA AAGGVGLAAI QIARLAGARI IATASSRKQG FVRLLGVEHV LDSRSLEFAE
QIRQITDGRG VDVILNSLAG EAIEKSLSIL ARYGRFVEIG KRDLYENRNL ALGFFREGIT
FHSIDLSRVM ADRPDLIRRI RGMLIEAFQS GRLHPLAHRI FAANRIRDAF RTMADARHVG
KIVISLRRPD IRVEPLPPVV APLHEQATYL ITGGTGGFGV EIARAMLCHG ARTIVLLGRS
DPSSEKVSRA LDRLSIFKNA RIVPIQVDVA DPVAMADVFR RMRDELPPLR GVVHAAGFLE
DGPVVQMDAA SFRRVLAPKV HGLWNLHELT RELSLDFFSI TGSSASLLGN AGQANYAAAN
AFLDTFAWFR SMSGLPANVV NFGPLTEAGM VARDPGLIDR MARLGVTMMP MRKGIEILRA
AQSRRQPQIG AIRVRWSRWL DAVGFASVPS KILDLYEKDA ATATAEQNSS ELLQSLRQAS
AGELPDLVMS YVASTIARVL GTQAEKLDPA QPLQALGLDS LATVELCNRI EGDLRITMPH
AELAKKPTLV QLAALVLSLL PQKAGA
//
