ID A0A0G3UEM1_9ACTN Unreviewed; 1632 AA.
AC A0A0G3UEM1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AKL64832.1};
GN Name=lnyHD {ECO:0000313|EMBL:AKL64832.1};
GN ORFNames=M444_04835 {ECO:0000313|EMBL:AKL64832.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL64832.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL64832.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL64832.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP011664; AKL64832.1; -; Genomic_DNA.
DR KEGG; strm:M444_04835; -.
DR PATRIC; fig|465541.12.peg.1145; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000035653; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 6.10.140.1830; -; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR041618; PKS_DE.
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; 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; 1.
DR Pfam; PF08990; Docking; 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; PF18369; PKS_DE; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1474..1549
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1595..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1616
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1632 AA; 170861 MW; 23CAA93CACFA6A22 CRC64;
MANEAKLREY LKKVTTDLDE AYGRLRDIES QAHEPIAITA MSCRFPGGVR SPEELWELLA
SGGDALTAFP TDRGWDLEHL FSDDPDDQGT STTREGGFLS GASEFDAHFF GISPREAMAM
DPQQRLLLET SWEAFERAGI DPNLLRGSQC GVFVGMNGSD YLTPLLEAAE DYAGHLGTGN
ASSVLSGRLS YTFGLEGPAV TVDTACSASL VALHLAAQAL RAGECSLAVA GGVHVMSTPG
LFVEFSKQRG LSTDGRCKAF AAGADGFGPA EGVGVLLLER LSDARKNGRP VLAVLRGSAI
NQDGASNGLT APNGPSQQRV IRQALANARL SADQVDVVEA HGTGTSLGDP IEAQALLATY
GQDRPADQPL LLGSVKSNIG HTQAAAGVAG VIKMVLAMQH GVLPQSLHID EPSPHVDWAA
GTVELLTEQT AWPERTHPRR AGVSSFGFSG TNAHVIVEQA PEVEAAEPEA GSGMPVVPWV
LSGKSAGALR GQAERLSGWL AGAAGVDPLD VGWSLASTRA GLDHRAVVFG DHAAGVSAVA
SAGLAAGVVT GSVVGGKTAF VFPGQGSQWL GMAAELLGSS PVFAARVEEC AKALEPFTDW
SLVDVLRGVE GAPSLDRVDV VQPALFAVMV SLAEVWRAAG VRPGAVIGHS QGEIAAACVA
GILSLDDAAR VVALRSQAIG RVLAGLGGMV SIPLPATEVR ERIAPWGEQR ISVAAVNGPS
SVVVSGEVQA LEELLASCEA DGVRAKRIAV DYASHSAQVE LLREELAGLL APIVPQPAEV
PFLSTVTGEW VKGPELDSGY WFRNLRQTVE LEQATRTLLE QGFGVFIESS PHPVLTVGMQ
ETVEDAGREA AILGSLRRNE GGLERFWLSL GEAYVRGVAV DWEAVFAGTG AQRVDLPTYA
FQSQRFWPEA APVEAGDASV ESAIDARFWD AVEREDVTAL AEALAFDAPD AIQSLGTVLP
GLSSWRRQSR EQSTVDGWRY RVVWKPQADA VTKPRLSGTW LAVVPEAPAG AAGDTVAAVL
RTLADRGAEV RTVTVAAGAA GREALTATLK DATAGAPAAA GVLSLLALGG DAAAHALSQA
LGDAEVAAPL WCVTRGAVVA GRSDRITDPG QALVWGLGRV ASMEQGGRWG GLVDLPGTDA
ADDRTLERLV GVLAGDAAED QVAVRSSGLF VRRLVRARLA DSPAVREWRP RGTTLVTGGT
GVLGGQVARW LAGNGAEHLL LASRRGAEAP GAVELREELT ALGARVTLAA CDVSDREALA
GLLATVPADQ PLTAVIHAAA VVDDGVIETL TAEQVAAVLR VKVDATRHLH ELTRDLDLSA
FVLFSSFAAT FGAPGQGNQA PGNAFLDAFA EYRRADGLPA TSLAWGPWGS ADGDDSAAGD
RMRRHGIIAM PPARTLASLQ HALDRDETTL TVVDMDWKRF TLAFTADRPR PLLLELPEAR
RVIESAERES AEDLAGGVPL TQQLAGLPDV EQERLLLDLV RTAVAAVLGH ADLTAVEAGR
AFKELGFDSL TSVELRNRLG AVSGLKLPAS LVFDHPTPAA VAAYLRAGIV PDAAAGGAPL
LEEIDKLESV LERGTADNVV RARVTMRLQS LLAKWSDTED PAEEDPADEA EQVQDASDEE
LFALINNGLG RY
//
