ID A0A0J7ZMB9_STRVR Unreviewed; 1112 AA.
AC A0A0J7ZMB9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Type-I PKS {ECO:0000313|EMBL:KMS77094.1};
GN ORFNames=ACM01_00135 {ECO:0000313|EMBL:KMS77094.1};
OS Streptomyces viridochromogenes.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938 {ECO:0000313|EMBL:KMS77094.1, ECO:0000313|Proteomes:UP000037432};
RN [1] {ECO:0000313|EMBL:KMS77094.1, ECO:0000313|Proteomes:UP000037432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3414 {ECO:0000313|EMBL:KMS77094.1,
RC ECO:0000313|Proteomes:UP000037432};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUN-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:KMS77094.1}.
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DR EMBL; LFNT01000001; KMS77094.1; -; Genomic_DNA.
DR RefSeq; WP_048578886.1; NZ_LFNT01000001.1.
DR AlphaFoldDB; A0A0J7ZMB9; -.
DR PATRIC; fig|1938.3.peg.3056; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037432; 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; 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; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..439
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 921..999
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 595..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1052
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 117806 MW; E1D97E2535F1D940 CRC64;
MTTSEPDPRM AVIGMAFRLP GGDTPEEFWR VIHEGTDCVT RFTDEELSAA GVPAEEYRAD
DFVGASGVVD DIAGFDAQHF AMSAREARLT DPQHRMFLEC AQHALENAGY PGERDGTRVG
VYASTGYHLY TLQNYLLNNV LPNEPPADWM AGMQVTVANH TDFTATRVAY RLGLTGPAVN
LQTGCSSSLV GVQAAAQSLL MGDCDIALVG ATAVHVPQVL GYRYVKGSIL SKSGRLRAFD
ARADGTVGGT GVLAVVLKRL ARAVADGDTI HGVVRGWGIN NDGADKTAFT APSAQGQRVA
IRQALRRAGV GADTIGYLET HGTGTLKGDP IEFDGATDAY REDTDRTGYC ALGSTKANIG
HLDVASGLAG LVKTLLVLKH GVIPPMANFS EPNPRLDLDN SPFYIPRTAR PWPESDVPRR
AGLTSLGVGG TNVHLILEQA PDAAPRPDAV APADVLLVSA SSEGALADNA RAFRDRLRQP
PAPHLADLVT TAALGRAHGR HRLAARGSTP AALADVLDAW LAGTAGATVT TGTAPQEGPA
RIALQFTGQG SQYPGMAGPL HERFPAVREM LDACEHHYRE LTGDSLLAAL RVDDEPEAGP
AGGRPPEEEP PWGTDTAQPA LFALQCALVR LWRDAGIEPY AVTGHSVGEY AALYAAGALT
LDDGLRLTTE RGRLMRQRCA RGAMVAATLD RESALALADE VPGLEVAVTN GEHAQVLAGT
VEAVDRACAL LDRRGTPGQR LAVTRAFHTA LMEPMLDEFR KILDDVAFRP VRIPFVSAVD
GVTRPPGWTP DADYFLRHTR RPVRFDEALR GIGAQQPDVL LEIGPHTTLS GLARRALPAV
PSLPSLRRGT GLGSLWGAAA GLHCAGADVG WPALLAGTGG RRIPLPGYRF QHKHHWTGPE
LTALSTGTPA SKGAEVVQQE AAVGRVLHSI VEATARHLGE DPSLIAGDAS FFDLGADSLL
MISVLRELEQ EHQVNVTMRQ LFEETGTPRR LAEFIVARMP GAPSGSASAE VPVERDELAD
PAAPRLTPPA TSPAPAPAPA QVPAPAPVFE PAPAAPASAS LPEYATREEL EDLAHKIQQM
SQIQLQMMSQ LSQLLALQTA SVTERLNGKV AK
//
