ID A0A0Q8ZQ96_9ACTN Unreviewed; 1049 AA.
AC A0A0Q8ZQ96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KRD08796.1};
GN ORFNames=ASE41_31210 {ECO:0000313|EMBL:KRD08796.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD08796.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD08796.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD08796.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD08796.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD08796.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRD08796.1}.
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DR EMBL; LMIZ01000038; KRD08796.1; -; Genomic_DNA.
DR RefSeq; WP_057581820.1; NZ_LMIZ01000038.1.
DR AlphaFoldDB; A0A0Q8ZQ96; -.
DR STRING; 1736503.ASE41_31210; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000051177; Unassembled WGS sequence.
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; 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 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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
DR InterPro; IPR009081; PP-bd_ACP.
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; 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; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 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; 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.
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:UP000051177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..465
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 971..1046
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 932..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1049 AA; 111139 MW; 6044230D40D5E2DE CRC64;
MTTAAPTGDE AKLLDYLKRM TVDLREARRR VQELDDAAHE PIAVVGIGCA YPGAVASPDD
LWRLLDTGAD AVGDFPTDRG WDLDALYDPH PDTPGTCYTR NGAFLPDAAS FDAPLFGITP
KEALTIDPQQ RLLLEHSWEA VERAGLDPRT LHGSRTGVFV GVMYNDYGAR LRPVPDGYEG
YIGSGSAASV ASGRISYSLG LQGPALTVDT ACSSSLVALH LACQALRRGE CTAALAGGVT
VMATPTVFTE FARQRGLSAD GRCRSFSADA DGTGWAEGVG MLYLERLSDA VRAGRPVLAV
LRGSAVNQDG ASNGLTAPHG PSQERVIRDA LADARLTPHD IDAVEAHGTA TTLGDPIEGH
AIQSVYGTGR DPQRPLYLGS LKSNIGHSQA AAGIGGVIKM VLALRHGVLP KTLHAERPTP
HIDWTATPVR LLQEPVDWPR TDRPRRAGVS SFGISGTNAH VIVEEAPQAT PPQATAPETT
APGTATPATA FAVPLSAHTP KALRAQAARL GAHLTARPGL ATGDVAHALV TSRTLFDHRA
VLVAPGRDAL LQGLDKLARG TGAPHTVRGA PDPAAKSPCA VLFSGQGSQR PGMGRDLYQR
FPAFADALDT ACAALDPHLE LPLHDVLFGT AQPQDLINRT AYTQAGVFAV EVALYRLLER
FGVTPGFVAG HSIGELTAAH VAGVWTLPDA ARLVAARGRL MQALPEGGAM LAVQATAAEL
QPLLAGREHE IALAAENGPA SVVVSGDTAA VQELDTHWRE HGRRTKRLQV SHAFHSPHMD
AMLDDFHRVA KELTYHRPQL PIISHLTGET SPEALLTPEY WVRHVREPVR FATGVRRLTA
HGVTTFVEAG PDSVLTPMVA ECLDGAPGDA VALSRRDQRE PEAFLAALAR LHVRGAAVDW
AAQHDGQTAA RAELPTYPFQ RRRYWLDEVT PATPRTAHGP ALQAPTTDQD PDGDETWAAR
LAAAAPADRH ALILTCVVEA AAEVMGADSP DTVPLGTPLL DLGFTSLMAV DLRNKVTQAT
GVDLPPTVVY DHPTFEAIAS HAHALMSTD
//
