ID A0A176L1G7_9ACTN Unreviewed; 1509 AA.
AC A0A176L1G7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:OAA98376.1};
GN ORFNames=A6P39_23125 {ECO:0000313|EMBL:OAA98376.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA98376.1};
RN [1] {ECO:0000313|EMBL:OAA98376.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA98376.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-2016) 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:OAA98376.1}.
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DR EMBL; LWRP01000113; OAA98376.1; -; Genomic_DNA.
DR RefSeq; WP_067049462.1; NZ_CP119133.1.
DR STRING; 710705.A6P39_23125; -.
DR OrthoDB; 9778690at2; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR001227; Ac_transferase_dom_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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 2.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..470
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1488..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1509 AA; 160249 MW; 819D94968F29F3BD CRC64;
MTQPQTPVAI VGMAVLLPGA PGLDAYWRNL RDGVDAIRDV PAGRWDAGYY RPGSADGPAV
ADQVYCRRGG FVDGLAEVEV TRYGIMPASV PGTEPDQLIA LDVAAAALAD AGGPERLPER
NRIGVALGRG GYLTPGLVRL DQRVRTARQL VRTLGELLPG LDSGQLDRIH AAFTERLGPD
SPESAIGLVP NLAASRIANR LDLRGPAYTV DAACASSLVA VDQAVTELAT GRCDMMLAGG
VHHCHDITLW SVFSQLRALS PTERIRPFHR DADGILIGEG TGVVVLKRLA DAERAGDRVY
AVIRGTGVAS DGRTAGLVNP DPGGQARAVR QAWQAAGLDP AAPDAIGLLE AHGTATPAGD
TAELATLAEV FGPARGAGAR PVLGSVKSMI GHTMPAAGVA GLVKAALALH HRTLLPTLHC
EDPHPALAAT RFRPLDRARP WESEARQVVR RAAVNAFGFG GINAHVVLEE APGGRTASRA
HRVPAPAAQV AEPEPVLLLA AHSPAGLAGL LDADDPAVLA AGLDPARPHP GAGPVRLGVV
APTAKRLALA RRAVAKGRAW QGRGDVWFRP GPLLGRAGGR LAFVFPGLEG EFAPRTDDIA
AHFGLPPLPG TDVRVDDVAR HGFGVVGVGR LLDQALRRMG VVPDAVAGHS VGEWTAMAAA
GLYSAAQVDA FMAGFDPDTV TVPGLAFAAL GTSAEHVRTT LAEQWPDSGI VLSHDNAPRQ
SMVCGPGAAV EAFVRSLRAH GVICQVLPFR SGFHTPMLEP YLAPIQEAAD RFRLHPPTVP
VWSGTTAAPF PAAEAEVREL FVRHLLEPVR FRELTEALYA AGHRVFVQTG PGRLTSLIDD
TLGDRDHLSV AANAAQHGGM AQLRRVATAL WTAGASVAPA LQPRATAAQA GRRPVRLDLS
GALVSLDGPE LDTLRAHLRP AARPASARFG DLDALTPRIP AAAELTALLR DTADTAAELI
TASRRRTPAA AVPTLAIPAA AATTVHVSPR TMPHLLDHCF FPQRPDWPDV EDRWPVVPAT
TLVRHMMDAA EAAAPGLRAV AVHGARFDRW LTATPPVDVQ VTVTPDPGRP DRVTVAFGPT
ARAVVELAPH HPAPPRPGPL PGAPERRPEH TAAQLYRDRW MFHGPGFQGL TDLTAIGERH
IRGVITTPAA PGALLDNVGQ LLGYWIMATR TERTVVFPVQ IRQLTFHGPH PAPGTQVGCL
LRITSLTDTV LEADAELTAG GRVWARITGW QDRRFDNDPT TRPVERFPER HTLSTGRPGG
WVLVHERWPD LASRELIMRN SLGGAERAAY ADRPPRGRRQ WLLGRIAAKD AVRQWLWQQG
EGPVFPAELR LLNDELGRPY VTGTHGRTLP PLDVSLAHRA EAGVAIVRPH TPQPGPGIDI
EEVTERDPAT LATALGPAEL RLLHRLSANG PDPQALWFTR FWAAKEAVAK AEGVGFDGRP
RDFTVLEADR DGSRLLVSGR LERAYTVHCA PAGNPPALPE RSYVVAWATG PGTDDDAPPD
DDAAEECPR
//
