ID Q8GGP3_STRAZ Unreviewed; 4437 AA.
AC Q8GGP3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE SubName: Full=Hybrid nonribosomal peptide synthetase / polyketide synthase {ECO:0000313|EMBL:AAN85522.1};
GN Name=LnmI {ECO:0000313|EMBL:AAN85522.1};
OS Streptomyces atroolivaceus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66869 {ECO:0000313|EMBL:AAN85522.1};
RN [1] {ECO:0000313|EMBL:AAN85522.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12446651; DOI=10.1128/JB.184.24.7013-7024.2002;
RA Cheng Y.Q., Tang G.L., Shen B.;
RT "Identification and localization of the gene cluster encoding biosynthesis
RT of the antitumor macrolactam leinamycin in Streptomyces atroolivaceus S-
RT 140.";
RL J. Bacteriol. 184:7013-7024(2002).
RN [2] {ECO:0000313|EMBL:AAN85522.1}
RP NUCLEOTIDE SEQUENCE.
RA Cheng Y.-Q., Tang G.-L., Shen B.;
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAN85522.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12598647; DOI=10.1073/pnas.0537286100;
RA Cheng Y.Q., Tang G.L., Shen B.;
RT "Type I polyketide synthase requiring a discrete acyltransferase for
RT polyketide biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3149-3154(2003).
RN [4] {ECO:0000313|EMBL:AAN85522.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15112993; DOI=10.1016/S1074-5521(03)00286-2;
RA Tang G.L., Cheng Y.Q., Shen B.;
RT "Leinamycin biosynthesis revealing unprecedented architectural complexity
RT for a hybrid polyketide synthase and nonribosomal peptide synthetase.";
RL Chem. Biol. 11:33-45(2004).
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DR EMBL; AF484556; AAN85522.1; -; Genomic_DNA.
DR BioCyc; MetaCyc:MONOMER-21901; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19535; Cyc_NRPS; 1.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd02142; McbC_SagB-like_oxidoreductase; 1.
DR CDD; cd00833; PKS; 3.
DR Gene3D; 1.10.1240.100; -; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 3.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 3.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..91
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1530..1605
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1928..2344
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2661..3083
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3930..4350
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 689..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1621..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2514..2548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2622..2657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3750..3818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4381..4437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2628..2646
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3760..3797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4437 AA; 466889 MW; 8845274278F013B9 CRC64;
MEPGTSPSGQ QDASGLAARV TAVMVRVLSA ARPDAQPVTA ACELRGLGLD SMTAARLWLA
VQGECAADVP LGWLTEATTV GEYAQRVADH ASQAVPVQGA GAVGAQVAAD PDALHEPFPL
TPLQEAYLIG KEPELQADAV GCHLYREFDV PALDTERLRA AWQRLVEHHD ILRATVTEDG
RQQITAQAPR WDLAVHGSAT RAEFTETATA VRARMSHHLF PAGHCPPFAI EVTLGPDGTG
RVHFGIDAIV TDGQGLDLLT AQWEACYADP SHLLPAPTAP LSVRDCVVAL DAARRTEAHR
RDLDHWVRRL RELPGAPGLF TADAPERGTG LSCVRRSSRT ARLTAAEWRS LRARAEELAV
SPTSLVLTVF TEALARHGAH EPFSLVVTTS RRPQLPPEAD HLVGPFTGTT FVEAVPPQQH
TFEEAARLTH EGLWQALEHS AVCGVSAQRA LRGGGPGPLP VVFTSMLDAA GRPRARGFAA
APVYAVSQTS GVWLDHQMWE QDGALHLRWD TADGCFAPGV VEAAFASLCN GLRALAVAGP
VVTRPLNDLQ QAYFVARAAG EPGPWRGCQV VVPYDTDERV DPVRLESAVV RLVEAYDVLR
SAVTQDGVVE VRAGAPRRWT VPVVAGGCPD EVRDAMAAAN FPLGRYPQFE VRVVRGDDGD
TVLMSMDLTL TDARGIHLTG RELMRLYADP AAEPRPAEAA RDSARDADEQ ARSRAHWQDR
LRALPPGVPL PGPRDADGPD RRVRLAGAPL ALRPLTDRCA EHGLSLDAVL LTAFTDVLAR
TYGTDFAVPV VRWDHGLDPQ RPGEFTALSW LPCAPRELSF TARARTYQEG LERDADVSGS
GLPELRRAVA RSGGAGYPVV YTCALDLTDR PLPGSVRAGQ WLSCTPDVFL DCITTVDAGQ
LQLAWDAVDG RAPQGGWSEL HAEYRRSVAR LADDAAAWQE PAGGDTSGAD DGEVRGAELH
KILHEWNDTT RAFPDDRLMH QLFEEQAAQQ PRAEALRWRG GGTMTYQELN RRANRIAARL
AAEDVGPETV VAVSVPRGPM MVAVVLGILK AGGVYLPMEP HLPAERAAVI LEEAHAEVVV
TTADREGWPV PDGYARVCAD AAVEGPHPAD ADNCPRPVTQ PHNTAYIIFT SGSTGRPKGV
AVAHRPVLNL INWCRRTFGF GPGDMGLCVT SLGFDLSVFD VFGLLGTGAA LYIADAEQQR
DPALLLDVLI EEPVTFWNSA PTTLAQVGPL LDTVGTAGTG DLRLVFLSGD FTPLPLPDEV
RAVFPRADMI SLGGATEATV WSNWFRIGAI DPAWRSIPYG RPIDNSRYHV LDEALRPCPV
GVEGDLYIGG ECLALGYVNQ PELTADRFIP DPFHEDPQER LYKTGDRALY YPDGNLSFQG
RADGQVKVRG FRVELAEIEH RLRAHDGVKD AVVLAREDGC GDRTLVAYLV ALPGSAPSGR
ELRGFAGQTL PEYMVPNFIG FLAGFPATAN GKLDRAALPW PLAKAHLTPP DRSADADPVG
SEAEAAVPVK ESAAEQPAVA GGAGPSVSVP SRDELCAEIA DLFAQALGVE SVDADTDLWD
QGATSFTMVR VSGSLQRSYK QRFPVSALLD NPSVSAIAGW VHAQLGGGAD AESTAAAEAE
TATSVDAETT ATTVTQTTAA SDERPDSGPG PVDFFATEER ERFKRQHWNR RPDEPGLPEV
PLGDARFEDE LHAWRASRRD FLDQPVPHRS FSRLLGLLRE TTGADGTGAL YPSAGDTYSV
QVYLHLTPDA VEGLDAGLYY YDPSRHSLRL LRSGVLPDRG AHFYYNRPVF DRSRFGIYLF
GQRHGIEPLY AEESLRYLTL ESGYMSQLLM LGQAAHGVGL CPIGALNTEQ LSQWLGLDEG
HVFLQAFLGG AAEHPQRTAG GTVPFFTEPT DSDGNSGSGD SSTVITDAVA PVSAAAEDAD
AEPPAHTAEP AAVIGMAGRL PGAGDLDAFW DNLVSGRTAI GPAPASRPET APSGARATGG
FLPHIDRFDS LLFHVSPQEA PALDPQARLM LESVWQCLDD AGHTADSLRR SAGRVGVFIG
SMWHDYRQQG ADRWNGGDSA EVAATASDIA NRVSHFFDFR GPSLAVDTSC SSSFAALHLA
VESLRRGECG AAVVGAVNLL AHPYHWGLLD GLELLAADAP PAAYAAEGSG WHPGEGVGVL
LLRPADAARR AKDTVHGLIE GTRIGHAGRA PRYGAPHTAA LADSLARALA DASVIPDEVD
YVECAAAGAG IADAAELEAL GSVLARCAGA SPVPVGTLKP NIGHLEAASG LSQLIKVLLQ
IRHGRIAPTL VSGELSPLVD WDGLPVELVD TPRALTPRAA DGRATVLVNA VGATGSYGHV
VVRAPHAHGT GPAAQDGLAG AGAAPSASGP RTVVLSAASP EGLTAAAGRL RDHLAGAGRA
LCLDDVAWTL QTGRASLGHR LTLSADGLDG VRAGLTAFLD GRACPGLATA AADPALAGVP
AGAQDLARAA GDWLRGHAVD FARLWSAPAR RVPLPVQDFT VLAQERHWLA APAARRPDGA
AGSAPAAPES GQSAPPASPQ VQDDRADRAQ EHVAACFAEV SGIPAEQLHP RVPLEHYGLS
SRLVARFNER LRQDVQGVSS TVLFEYPDLA GVAAHLAAHH EGPWSAAPDT QPSPPVPSPD
PLPVPRTPAA ALGESAAADG PEPIAVIGIA GRYPGAGDLE TFWSNLAEGV DSVGPLPAER
ARDGWPTEQM WGGFLDGVDR FDALFFGIAP RDAQLMDPQE RQFLQVVWET LEDAGCTRAR
IREQLGSDVG VFVGTMYNEY PFFGVERSLA GESADTGSAV AGIANRVSYF LDLHGPSLAV
DTMCSSSLTA LHLAVESLRR GECAAAVAGG VNLSLHPHKF RQQTRLKMSS SDHRCRSFGA
GGDGFVPAEG VGAVLLKPLS AAEADGDRIH AVIRGTAVNH GGKTNGYMVP NPVAQGDLVR
AALRRAGADP ATIGYVEAHG TGTQLGDPVE INGLNRAFAG ASVAPASRAI GSVKANIGHA
EAAAGIAGLT KVVLQLRHRH LVPSLHTEEL NDAVDWASSP FEVVREGRPW APLTGADGAP
LPRRAGLSAF GAGGANAHVV VEEYVPGTAP EPTEPGVPGV LEPQLIVLSA HDLGRLRALA
GRLRDRLGRD DRPAPALADV AHTLQSGREP LRERVALVAY DVAGLCRALD LFASGDTGAW
VHGRTPGGAL PDGPKAVLDA AADRDAELLR LGRHWTGGGT VDWPGLHPVR RRLVSLPSYP
FAEDRHWLPE PRTAAPAAAA ATLTEPSGTT LYGRTWRALP PLAAAAAPAP SGRVLCVFSA
PGEPVARALA ALLGPDRVTL VRAGADAGNG VPGITGIGDE AEAAAFAQGL RADGPDAVGG
LIDLTDLGGP AHGDAGSWTA RLVLLRRLVR TLRGHGGRVL HVTEGLYGPA GPAPSLAGAR
MAGFVRMLGA EYGRVTGTVL DLDVSAVGPD AAARQILAEY TGPYGPGDVS VRGGVRHRPE
LVALPDAGHR SLTPAVDRAY LVTGGTRGIG ARVARLLVRR GARRIALTGA RPQPPRADWP
LLSPGTPEAE TASLVAELEA QGARVLVHSG PLSERERTDR FLREVREVLG PIGGVVHCAG
RGPVGRPSFI GKELADFDPV LEPKTTGLEV LDELCAGDRP EFFVLFSSLS AVAPGLAAGV
LDYAAANAFL DCYADHQVRS GRPWFRSVAW PTWSESGMGA DRPDSCAPVG VGPLGDEEGL
RVLERILALP AEQARIVPCP PIDGIAADPA ALLGSPRDTD ATASVGSTTS AGSTPMAGST
PMAGSTPAAG SAPVPTTTGA TPPRPREEEH TVPNTSVTGP PWLAPLFSEL LAIPEDALDP
TALLGDLGVE SVLLGEILLR LEELTGLSLD PATLLDHPTL ELLGRHLADL GVPSAPPAPA
ATTAPAVAPV TPVTPTAPVA VAPVTPVAPS GKIAVIGLSC RFPGAEDAAA FARNLLGGTC
SVTEVPPSRW DVGELYRPEL EPGRSTSKWG GFLDGIEDFD PEWFGMSEDE ARCLDPAVRL
FLEGSATCLT DAGYGARELA GRDVGVFAGA RMSHYGRRVG ERRGLVGMGS DQNFIAARIA
HHFDLHGPNL VVDSACSSSL VALQLACRSL LDGESELALA GGVDVLLDEE PYLDFSAAKA
LSRHGRCATF DEDADGFVPG EGCGVVLLKP LEKALRDGDR IHAVIDAVAV NNDGRTMGLT
TPNPAAQAKV VRRALAAAGR RADEVGLIEA HGTGTMIGDP IELRALTEVF REETGRTGFC
AIGSVKTNVG HLLSAAGMAG LIKAVLAVRD GRIAPTLFCE RPNPRFDFAA SPFYPSRTAH
DWVPEPGRVR VAGVSAFGLG GTNAHAVVSQ LDPVLAAAHR PRPALPAPNF ARRRLWLEAA
PPSAPGPRPS VPGRPPLGAS ILGLTFEEPL SEPGYAPLTP TPTGADTAAA SQEGRKW
//
