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Database: UniProt
Entry: A0A176L1F9_9ACTN
LinkDB: A0A176L1F9_9ACTN
Original site: A0A176L1F9_9ACTN 
ID   A0A176L1F9_9ACTN        Unreviewed;      2333 AA.
AC   A0A176L1F9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OAA98375.1};
GN   ORFNames=A6P39_23120 {ECO:0000313|EMBL:OAA98375.1};
OS   Streptomyces sp. FXJ1.172.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA98375.1};
RN   [1] {ECO:0000313|EMBL:OAA98375.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA98375.1};
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:OAA98375.1}.
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DR   EMBL; LWRP01000113; OAA98375.1; -; Genomic_DNA.
DR   STRING; 710705.A6P39_23120; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
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; IPR013785; Aldolase_TIM.
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; IPR004136; NMO.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
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; 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; PF03060; NMO; 2.
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   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
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; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          721..1159
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1724..1810
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          285..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1690..1724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1812..1863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1690..1720
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2333 AA;  240173 MW;  ECB2ECE81AECEEB1 CRC64;
     MTSPVRAHDL ILCLTPFGEP DARLAAAACA AGGLGILDLG SGDRRSREEL SRLGRAAPGP
     FGIRVTGRCA LSPADVAGAP DTVVLTPDAT WKVTKLPPEY RVLMEVTDLG QARAAVRAGA
     RGLIARGGES GGRVGELSTF VLLQQLLSDG ELSGVPVWAC GGIGPRTGAA AVAGGAAGVV
     LDSQLGLLPE SGLPESVRAA LRSLDGSETV VLGGHRVLRR RGPESPQPPA DDPGTVASLL
     GAGTPHAQLL PVGQDGFLAA RFAERWGDVR GVVREMSAAI QYVTHTGPMT TPGTPEPTAA
     ADGGARTVPA VSRDAADAGP AVSRDVADAG PVVARGAGRP GPADALRAGS GMCRVLGTRL
     PVAQGPMTRV SDQAGFAAAV AEGGALPFLA LALADGERTR AMLTEARGVL DGRPWGVGVL
     GFAPEEIRNA QLDAVRELRP THAVIAGGRP AQAETLERAG IRTFLHVPSP GLLRQFLEAG
     ARRFVFEGSE CGGHVGPRAS FPLWEAQLAV IEDYFAAAGD EAIRQLEVFF AGGIHDERSA
     AMVAALAAQL TARGAAVGLL MGTAYLFTTE AVAHGAIRPL FQRQVLTATA TALLETAPGH
     ATRCVPSPFT GDYRDREAAL RAGGLTDREV WEGLERLNVG RLRIASKGVE RDADGALAAV
     GEERQLTDGM FMAGQVAVLR ATTTTVADLH RAVTDGAADF LTRRAARPAP PATDEPPAPA
     PLDIAIVGMA CMFPEAPDLA AFWANVVTGR DAVTEVPPER WDPAVHHSAG RTASKWGGFL
     PRIPFDPLRY GIPPASLGSI EPVQLLSLEA ARRALEDAGY GERGRAFDRA RTSVVFGAEA
     GSDLSNAATL RAVLPAYYGR VPEGIEEQLP RLTEDSFPGM LANVISGRIA NRLDLGGANF
     TVDAACASSL AALDVACKEL VSGTSDLVLC GGADLHNGIN DYVLFSAVHA LSPTGRSRAF
     DSSADGIALG EGVACLVLKR LTDAERDGDR IYGVVKGLGS ASDGRSLGLT APRPEGQRAA
     LERAYRNAAV SPADVGLVEA HGTGTVVGDR TELTVLSEVF TEAGASAGSC ALGSVKSQIG
     HTKCAAGLAG LIKTTLALYT AVTPPTLHLE RPNPAWTQGD SPFAFHTRAR PWTAPAAQRF
     AGVSAFGFGG TNFHAVLAAH TRAVPPAQSL DAWPCELLLF RGRDTAAAHR TVAEILRAAE
     ADGRPWRLRD LALAAARRAD TAHEPVRAAV VARDIEELTV QLRRILAGDH DPAAGIHGAD
     PVPGETAFLF PGQGSQRTGM LADLLVTLPE LRHFLHLGRA HAEAVHPPAA FDDTARERHR
     AALTDTRAAQ PALGIAGLAA HAFLTSAGVH PDQAAGHSYG ELAALAAAGA LDPETLLELS
     GARAGAILAA AGDDPGTMAA VGAPAAAVTD VLRTAEAPAS VVVANLNSPE QTVISGPTAD
     VATAVRLLRA AGLGAKRIPV ACAFHSPLVA AAGERFAKIL ADKTVRAPEF PVWANRTAAP
     YPADPDAVRA ELAAQIGAPV DFAAQIEAMY EAGARLFVEA GPGTVLTRLV GQILGDRPHR
     TVACEPEAGS GLRGWLDALA RLAVAGQPVR TAWLLRGRDA VDALRAPAPE RPGWTVDGHL
     VRTADGALLP GALAPARRVV ETTVTTDQPS GAPTDRDALI SEFLRTSREM IAAQRDVLLT
     YFGATPGAAP APAPVPPPVS PAVQPAAREL PPPEPQLPLL PATGPADDVD RVVLEIISER
     TGYPVDMIEP DLDLEADLSI DSIKRAEIAG ELAKRLGIAA GAEVLADAEL EELAKARTAA
     AVTQWLTARA GAGTGAGGGG EPAGERAQTS YPGARTQEPA SVQGVPPRRC ELRPVPLPEP
     GPADAGLSGR RFALLGGEGV AAAVAARLTG HGADAVLLDR GHLLTEADGP VDAVVYLGAL
     PGPGLPALPD AFPVLRAALA CGPRALLAVR AAERAPALRA AGLDGLLRTV GREYPGLLAR
     IVAVPDTAPA AVAEAVLAEL CAPQPAAPVV LRTAAGTRQG LELVPVPLGP LGTTGAGPAA
     DGAAEAAALG LDRDSVVLLA GGARGITARF AATLARACRC RLELLGRTAA PTAPEDPRTA
     AARTPAELRA ALAAGPDAPT PAEINRAAEL TLAQREITTT LAELGALGSE ARYRAVDFRE
     RDAVLQAVKE IHAEHGRLDG VVFAAGVIED RLIADKTPES FQRVYGTKTA GAAALFAALD
     DLPAAPAFTV LFGSIAAVLG NRGQADYAAA NDALEALGAD WAARTGHRAL TVHWGPWAPS
     GTHTGMVGEE LGREYARRGV GLIDPDEGTA ALLRELAWGD PAARAVVHTA SGW
//
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