ID Q9F7T9_STRAX Unreviewed; 3626 AA.
AC Q9F7T9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Avermectin polyketide synthase {ECO:0000313|EMBL:AAG09812.1};
DE Flags: Fragment;
OS Streptomyces avermitilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=33903 {ECO:0000313|EMBL:AAG09812.1};
RN [1] {ECO:0000313|EMBL:AAG09812.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC31271 {ECO:0000313|EMBL:AAG09812.1};
RA Hong Y.-S., Lee J.J.;
RT "Targeted Gene Disruption of the avermectin O-methyltransferase gene and
RT polyketide synthase gene from Streptomyces avermitilis.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; AF275943; AAG09812.1; -; Genomic_DNA.
DR SMR; Q9F7T9; -.
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; 2.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 6.10.140.1830; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR041618; PKS_DE.
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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 3.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF18369; PKS_DE; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 3.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 3.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 3.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 354..436
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 461..874
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1956..2031
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2052..2479
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 987..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2480..2505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3458..3490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 3626
FT /evidence="ECO:0000313|EMBL:AAG09812.1"
SQ SEQUENCE 3626 AA; 380563 MW; 6272F5F088C1A8D0 CRC64;
MADEADGGVV FVFPGQGPQW PGMGRELLDA SDVFRESVRA CEAEFAPYVD WSVEQVLRDS
PDAPGLDRVD VVQRTLFAVM ISLAALWRSQ GVEPCAVLGH SLGEIAAAHV SGGLSLADAA
RVGDAWSQAQ TTLAGTGALV SVAATPDELL PRIAPWTEDN PARLAVAAVN GPRSTVVSGA
REAVADLVAD LTAAQVRTRM IPVDVPAHSP LMYAIEERVV SGLLPITPRP SRIPFHSSVT
GGRLDTRELD AAYWYRNMSS TVRFEPAARL LLQQGPKTFV EMSPHPVLTM GLQELAADLG
DTTGTADTVI MGTLRRGQGT LDHFLTSLAQ LRGHGETSAT TVLSARLTAL SPTQQQSLLL
DLVRAHTMAV LNDDGNERTA SDAGPSASFA HLGFDSVMGV ELRNRLSKAT GLRLPVTLIL
DHTTPAAVAA RLRTAALGHL DEDTAPVPDS PSGHGGTAAA DDPIAIIGMA CRFPGGVRSP
KDLWELAASG GDAIGPFPTD RGWPTEQRHA QDPTQPGTFY PQGGGFLHDA AHFDAGFFGI
SPREALAMDP QQRLLLETSW EAFERAGIDP LSVRGSRTGV FAGALSFDYG PRMDTASSEG
AADVEGHILT GTTGSVLSGR SAYSFGLEGP AITVDTGCSA SLVTLHLACQ SLRSGECTFA
LAGGVSDVHP GMFIEFSRQC GLSVDGRCKA VSAAADGTGW GEGIGLLAVV RGSAVNQDGA
SNGLTAPNGP AQERVIRQAL ANAGLSVADV DVVEGHGTGT TLGDPIEAQA LLATYGQRAG
DRPLWLGSLK SNIGHTMAAA GVGGVIKMVM ALREGVLPRT LHVDEPSPQG LAAGAVRLLT
EAVPWPGDAA GRLRRAGVSS FGIGGTNAHV ILEEAPAAGG CVAGGRVLEG APGLAISVAE
SVAAPVAVSA PVAESVPVPV PVPVPVPVSA RSEAGLRAQA EALRQYEAVQ PDVSLADVGA
GLACRQAVLE HHVVILAACT SSSRSAARTT ARSSSTARPQ ARPAPTSARR IGALAAGSGS
AALTTGHAPG GDRGGVVFVF PWQGGQWAGM GVRLLCLLRV FARRMQACEE ALAPWVDWSV
VDILRRDAGD AVWEQADVVQ PVLFSVMVSL AALWRSYGIE PNEVLGHSKD EIAAAHIYGA
LSLKDAAKTV ALPPQEVEQL IGERGGRLWV AAVNGPRSTA VSGDAEAVVE VLAYCAGTGV
RPRIPVDYAS HCPHVQPLRE ELLELLGDIS PQPYGVPFFS TVEGTWLDTT TLDAAYWYRN
LHQPVRFSHD VQALADQGHR VLLEVSPHPT LVPAIEDTTE DTARRRHCDR QPPPRRERHP
LLPQRLRLDP YYRHRQTHHV APLLDPPRHL PPPLDAPRPA HLPFQHQHYW LESSQPGAGS
GSGAGAGSGA GSGRAGTAGG TAEVESRFWD AVARQDLETV ATTLAVPPSA GLDTVVPALS
AWHRHQHDQA RINTWTYQET WKPLTLPTTH QPHQTWLIAI PETQTHHPHI TNILTNLHHH
GITPIPLPLT THHTNPQHLH HTLHHTRQQA QNHTTGAITG LLSLLALDET PHPHHPHTPT
GTLLNLTLTQ THTQTHPPTP LWYATTNATT THPNDPLTHP TQAQTWGLAR TTLLEHPTHT
AGIIDLPTTP TPHTLHHLTQ TLTQPHHQTQ LAIRTTGTHT RRLTPTTLTP THQPPTPTPH
GTTLITGGTG ALATHLTHHL TTHQPTQHLL LTSRTGPHTP HAQHLTTQLQ QKGIHLTITT
CDTSTPRPTH NNSLNTIPPQ HPVTTVIHTG GILDDATLTN LTPTQLNNVL RAKAHSAHLL
HQLTQHTPLT AFVLYSSAAA TFGAPGQANY AAANAYLDAL AHHRHTHHLP ATSIAWGTWQ
GNGLADSDKA RAYLDRRGFR PMSPELATAA VTQAIADTER PYVVIADIDW SKIEHTSQTS
DLVSAARERE PAVQRPTPPA ELHKTLAHQT SADQRAALLE LVRDHVAAVL RHADPKAIAP
DQSFRALGFD SLTAVEFRNL LIKATGLRLP VSLVFDHPTP AKLAVHLQNQ LRGTAAESAP
SAAAVTAEAS VTEPIAIVGM ACRFPGGVTS ADDFWDLISS EQDAIGGFPT DRGWDLDTLY
DPDPDHPGTC YTRNGGFLYD AGHFDAEFFG ISPREALAMD PQQRLLLETA WETIEHAGIN
PHTLHGTPTG VFTGTNGQDY ALRVHNAGQS TDGFALTGTA GSVISGRISY TFGFEGPAVS
VDTACSSSLV ALHLACQALR AGECSMALAG GVTVMSSPGA FVEFSRQRGL AADGHCKAFS
AAADGTGWGE GVGMLLVERL SDAHRNGHRV LAVVRGSAVN QDGASNGLTA PNGPSQQRVI
RQALANAGLS AGDVDAVEAH GTGTTLGDPI EAQALLATYG QDRAGEGPLW LGSVKSNVGH
TQAAAGVAGV IKMVMALRHG LLPRTLHVDE PSPHVDWSAG AVQLLTETVP WPGGEGRLRR
AGVSSFGVSG TNAHVILEEA PADDVPGGPP AGEGDAGSDD EAAAGSPGVW PWLVSAKSQP
ALRAQAQALH AHLTDHPGLD LADVGYTLAH ARAVFDHRAT LIAADRDTFL QALQALAAGE
PHPAVIHSSA PGGTGTGEAA GKTAFICSGQ GTQRPGMAHG LYHTHPVFAA ALNDICTHLD
PHLDHPLLPL LTQNDNDNED AAALLQQTRY AQPALFAFQV ALHRLLTDGY HITPHYYAGH
SLGEITGAHL AGILTLTDAT TLITQRATLM QTMPPGTMTT LHTTPHHITH HLTAHENDLA
IAAINTPTSL VISGTPHTVQ HITTLCQQQG IKTKTLPTNH AFHSPHTNPI LNQLHQHTQT
LTYHPPHTPL ITANTPPDQL LTPHYWTQQA RNTVDYATTT QTLHQHGVTT YIELGPDNTL
TTLTHHNLPN TPTTTLTLTH PHHHPQTHLL TNLAKTTTTW HPHHYTHHAQ PTPHPHPLDL
PTYPFQHHHY WLESTQPGAG NVSAAGLDPT EHPLLGATLE LATDGGALLA GRLSLRSHPW
LADHAVGGTV LLSGATFLEL ALHAGTYVGC DRVDELTLHA PLVVPVDGGV SVQVGVAAAD
GKGRRLVSVY ARGGSACGGG GASGGVWTCH ASGVLVEAAA GGVVVDGLAG VWPPRGAVAV
DVDGVRDRLA GAGCVLGPVF SGLRAVWRDG GDLLAEVCLP EEAWGDAAGF GLHPALLNGV
VQPLSVLLPG GTGFGKGAGF GKGVRVPAVW GGVSLHRAGV TGVRVRVSAV GRGGGREAVS
VVVGDEAGVP VASVDRLELR PVDMGQLRAV SVSAGRRGSL YAVQWAEVGP VPVCGQAWAW
HEDVGESGGG PVPGVVVLRC PDAGAGGGGG GGGGGGVGEV VGGVLGVVQG WLGLERFAGS
RLVVVTRGAV VAGPEDGPVD VVGASVWGLV RSAQAEHPDR FVLLDLDTDT GTDLDTGAGA
GWGVDGGRVA AVVACGEPQL AVRGERLLAA RLTRLESSGD VPAQRSGDTR ARRSDVPAQR
SGGVPARRSV DVSGREVLPW LSGGSVLVTG GTGVLGAAVA RHLAGVCGVR DLLLVSRRGP
DAPGAEGLRR SWPRGAEVRI VACDVGERRE VVRLAGGCSC RVSVFVDFSA VASVTVRLPV
ASDVRKEAAM AYATVEEFTD YLDPDP
//
