ID A0A2V2PYB6_9ACTN Unreviewed; 1155 AA.
AC A0A2V2PYB6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PWS40731.1};
DE Flags: Fragment;
GN ORFNames=DKT74_31305 {ECO:0000313|EMBL:PWS40731.1};
OS Streptomyces sp. ZEA17I.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS40731.1, ECO:0000313|Proteomes:UP000245984};
RN [1] {ECO:0000313|EMBL:PWS40731.1, ECO:0000313|Proteomes:UP000245984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZEA17I {ECO:0000313|EMBL:PWS40731.1,
RC ECO:0000313|Proteomes:UP000245984};
RA Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT "Genome sequencing and identification of chitinase family genes of
RT Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:PWS40731.1}.
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DR EMBL; QGMS01001599; PWS40731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2PYB6; -.
DR Proteomes; UP000245984; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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; 3.40.50.720; 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
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; 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; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 263..338
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 372..798
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 340..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PWS40731.1"
FT NON_TER 1155
FT /evidence="ECO:0000313|EMBL:PWS40731.1"
SQ SEQUENCE 1155 AA; 120851 MW; AEB1468855E2A392 CRC64;
ATHLVLPGRR GPQAPGASEL TAELAALGVR LTLPVCDLSD RQAVAELLTG LETAGDPVTA
VVHAAAFVAL APLDGTPMSA FEQIVAAKAA GAEHLDALLD RELDAFVLFS SIAGVWGSGD
HGAYAAANAY LDALAQHRRA RGLTATTIDW GIWQAENPWQ DRVAAEDADL FNLEQHGLPR
IAPDVALHAL RQALDDDETV LTVADVDWER FAAVFTSARP SPLLTGIPEA RRALEATAGE
AEAPAAALLR QRLAALVESE QHRLLLDLVR THAAAVLGHA TVDAIRPGRA FQDLGFASLT
AVELRNRLNA ATGLRLPSTL IFDHPSSTAL AREIRTELLG RRTTDPDPSA PHLSDPARSV
TDAAAHPPAP DDEPIAIVSM ACRFPGGIGT PEELWRLLAD GGDAVSDLPT DRGWDIEALY
DPDPDHPGTS TTRHGGFLHD AADFDAEFFG ISPREALAMD PQQRLLLETT WEAIERAAID
PAALRGSRTG VFTGVNYADY AAVVAQSEEG DGHLLTGSAP SVVSGRVAYT LGLEGPAVTI
DTACSSSLVA LHLAGRALRG GDCSLALVAG VAVMATPGAL ISFSRQRGLA EDGRCKAFSD
DADGMGMGEG VGVLLLERLS DARRNGHPVL AVVRGSAVNQ DGASNGLSAP NGPSQQRVIR
AALADAGLTA ADVDVVEAHG TGTTLGDPIE AQALLATYGQ DRPAERPLLV GSLKSNLGHA
QAASGVAGVI KTVLSMRHGQ VPRTLHVGRP SCHVDWTRGA LALATEQQPW PLHRGRPFRA
GVSSFGLSGT NVHTILEHAP QDDDGPPAER APLPTVPWLL SAKSPQALRA QADRLRRHLD
GSPASDPRDI GSALNTRTAF ECRRVLIGDR DQLRTLLGEM ADDASGAGDG GRTADGRSVL
VFPGQGSQWV GMAAELLGES GVFAGRMAEC ERALAPYVDW SLAEALGSER LLARVDVVQP
VLWAVMVSLA EVWRSFGVAV DGVVGHSQGE VAAACVAGGL SLEDGARVVA LRSRAVGVLA
GRGGMASVPL PVDVVRERLS GWGGRLSVAA VNGPSSTVVS GDADAVAGLL EALAGEGVRA
RRVEVDYASH SLHVEEIREQ LLSDLAGITP QSGAVPFFST VTGGWLDTKG LDAEYWYRNL
RETVELGKAT EALLS
//
