ID A0A069K4A2_9ACTN Unreviewed; 3156 AA.
AC A0A069K4A2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KDQ71030.1};
GN ORFNames=DT87_28640 {ECO:0000313|EMBL:KDQ71030.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ71030.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ71030.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ71030.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:KDQ71030.1}.
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DR EMBL; JJOB01000001; KDQ71030.1; -; Genomic_DNA.
DR RefSeq; WP_037881382.1; NZ_JJOB01000001.1.
DR OrthoDB; 5478077at2; -.
DR Proteomes; UP000027475; 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:0043604; P:amide biosynthetic process; IEA:UniProt.
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:0046483; P:heterocycle metabolic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 1.10.287.490; Helix hairpin bin; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
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 10..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1748..1829
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2846..2921
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2453..2473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3156 AA; 341550 MW; 985FBF14B518A703 CRC64;
MADAINNPLR SKVAIIGMGC RLPGGASDHR TFWRNLMEGR DCITPTPPDR YDVTTLGSRH
RDKPGRLTGG RGGYIDGFDE FDPAFFGISP READHMDPQQ RKLLEVAWEA LEDGGQRPAE
LAGSDVAVYV GAFTLDYKIL QFSDLGFTSL AAHTATGTMM TMVSNRLSHC FDFRGPSLSI
DTACSSSLVA VHLACQALDR GESDLALAGG TLLHMAPQYT VAETKGGFLS PEGRSRTFDA
SADGYVRAEG VGLVALKRLE DAVRDGDRIH AVILGSGVNQ DGRTNGITVP NAEAQVSLIR
RVCAEAGITP GGLQYMEAHG TSTPVGDPIE ANALARALAV GRAPGDRCYV GSVKTNIGHT
ESAAGIAGLI KTVLCLKHRY IPPHINLEHL NPAIDADALS YEIPTRPTAW PEHEGPARAG
VNSFGFGGTN AHVVLEEAPP AAPDGPAMTA GPVTTTAAGP PADRCAPTTA DARGWSILPL
SARHPDALGD LAAGITGELA GGDGRAPVSL ADLGHTLAHR RQHLTERLSV VYTSRASLDE
ALTAYRRGEP HPRVVQGRLR AAEDRRLVWV FTGMGPQWWG MGRQLLREEP AFREAVTECD
RVLGQFTDWS LLAEMSATQS ASRMGETWLA QPANFAVQIG LAALWRAYGV RPDAVAGHST
GEIAAFYEAG VYSLEDAVRI VVHRSRLQQT LAGTGTMLAV SLSEDEAEQR VRPYRDRVSI
AAVNSPTSLT LAGEEEALTL LAEELRAEQL FAKFLTVEVP YHSVGMERIK DDLFEALAGL
TPRPARVPLY LTGQEGTAEG PELDAAYWWK NVRDRVRFRA AVDRLADDGH QVFLEIGPHP
VLAHSIRECL DARAASGLTL PSIRRQEDES ERFAASLASL HNLGTGIAWD TLQPAGRPVT
LPRYPWKRDR HWTEPAAVAQ VRLGRLDHPL LGRRTDHAEP TWQARLDTET LPYLADHRVQ
DTVVFPAAGY LEMAAQAVLR ITGGTRTVLA DVDLRKALFL SDTEDRTVQL SLSLEDAAFT
VASPAAGDGE RTVHASGVVR TGQRRDPGPP LDAAAIRART DRHLAGPDCY AALARLGYHY
GPAFQAIEEV WIGPGEVLAR IRPPQAIGGD AARHHLHPVL LDACFQSLLT PQTLREDTAP
GDGIRLPLSL DEVALEPVGD QPLWVHATLL PSDKDTTLGD IALYADDGSP LGRISGFRAA
DVEKAVTTVA RTTIDSWLAE TVWTEAPPQP AEDADAAAAA RDHGWLLLAD GQGVADAFAA
LAAARGERCH LVRRGDGYTE GGMGGALTVD PGSPADLERL FAHLDRQGGP FRGAVLHLWN
LDRPALARCD RRALGDHTGP GAYSLVALAR TLLARGGAGR LHIVTRGAQP VLPGEAVEPL
GAPAWGIGRV LRHQELIDHP GKLIDLDPRQ RPGPDGVRAD AEALLREVLT GDEEEVALRA
GDRRTSRLSP AAGLTRPLPL RLRADGSYLV TGAFGALGRL LCRTLVRRGA RRLILVGRTP
VPAREKWSGA DPTAAEGRAV ALLRELEDLG AQTVLAPLDI TDEDALTGWL DAYRSTDPPP
VRGVFHLAGQ VRDTLVTDLD RSTFDAVHDP KTVGAFLLHR HLRDEPLDHF VLFASIASLL
TTAGQTNYAA GNAFLDALAH HRRAQGLPAL SLDWGPWATG MIEELGLVDH YLHSRGMSSL
APEAGMGVLE RVIGQDHAQL VVATVVDWPV FLAWYPAPPP LVAGLAAAAA PPASGGSGNA
FLDAFGAADE ETRRCLVAER FAELAAAVLR TTAESVDMAA GLGALGLDSL LAMELRARVH
AELGVALPVV ALLSGTPAGE LAAQLHDGLS ALVAAEDSGD GARAVEPHRD ESRYPLTQNQ
KALWFLKHLN PDGYAYNIGG AVEVTVALEP DLMFEAVRRL IARHPALRTN FVLEDGRAVQ
RVSPDAEPDL ALFDVRDQDW DAIHRTIVAE YRKPYDLAHD PLVRFRLFRR GPERWIIMKA
VHHIVSDAIS TFTFIEELFE VYEALRQGQE PQLPPPAARY LDFLNQQNQF LAGREAAGML
DYWRSHLPAE VPLLDLPVDK PRPAVQTHNG ASEFFELDTG LSARVHALAR AHHVTPFMVL
LSAYYLLLHR YSGQDDIIVG SPVTGRTRQD FASVYGYFVN PLPLHADLSG DPTVAELLEQ
VRTTVLGGLD NQEYPFVLLV EELGLQHDPS RSAVFQAMFI LLTHKVATEQ YGYKLDYIEL
PEEEGQFDLT LSVYEDESEH RFHCVFKYNT DLFLAETVRR MASHYTRLLD RMTRAAEDRP
TSRLEMLDDT ERERLVGRWG RPALPAPGTS PESTGGQEPF LPVHVRIGRV AAARPEAVAV
TVPAPDGGAR RMTYAELERR AGECAHRLRA RGVTTGSVVA LRLDKSPELI VTLLAVLKAG
GAYLPVQPDQ PADRLAHLLR ITGAVLLVTD GTTGQEPSEG LPVATVTLDA LHATGPEPHT
SPAPEDEVGP GSPAYVITTS GSTGRPKAVR VGHGNLASAY TAWRDTYHLE EDVRVHLQMA
GPSFDVFTGD LVRALCSGGN LVLADRDLLF DTPRLYRTMR QEYVDCAEFV PAVVRGLMDH
CVREDLRLDF MRLLVVGSDA WNVGEYRRLG ELCGPETRVV NSYGLTEATV DSAFFEGPAD
ALEPGLMVPI GRPLPHSTLH VLDPHGEPVP PGVPGELWIG GDGVALGYAG DPEQTARRFV
TRTLSRRPGA TPERFYRTGD IARWDAHGRV HLLGRTDGQV KLRGHRIETG EIEAHLHRWP
GLARAVVTVR ADTRKDPALC AYCVPAPGAA LDRRALRRHL AGALPSYMIP SYFVEMSALP
LTSNGKVDLA ALPAPRAETR ERTHEPPTTL YEVSVARHWK TLLGLEQVGL EDDFFDVGGS
SVKLIELLHH LRTEFGVSVP VSRLYRTTTL HGMAATVQEV LHGTSADELP YLSFNGGQPR
LLFAFPPAGG HGLVYRGLSA HLPEYTVIGF NYLPGDDKVT RYADLIESAR PEGACLLLGY
SLGGNLAFET AKELERRGRQ VAHVVVLDSR RILEPYEPGD EGIRVFEAEL AEHLRKHTGS
EAVARETLAH AAEYLAFCGR TPNTGTVTAA VSVITDEEKA SLYAAGERGT WHGSSAGTTT
VLRGSGTHAD MLDPKHLARN AELVRAVLTG DAAHGG
//
