ID A0A291Q3D3_9ACTN Unreviewed; 3995 AA.
AC A0A291Q3D3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:ATL26241.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:ATL26241.1};
GN ORFNames=KY5_1223c {ECO:0000313|EMBL:ATL26241.1};
OS Streptomyces formicae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL26241.1, ECO:0000313|Proteomes:UP000221011};
RN [1] {ECO:0000313|EMBL:ATL26241.1, ECO:0000313|Proteomes:UP000221011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY5 {ECO:0000313|EMBL:ATL26241.1,
RC ECO:0000313|Proteomes:UP000221011};
RA Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT producer.";
RL Submitted (AUG-2017) 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; CP022685; ATL26241.1; -; Genomic_DNA.
DR KEGG; sfk:KY5_1223c; -.
DR Proteomes; UP000221011; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
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; 2.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF08990; Docking; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 2.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 5.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
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; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:ATL26241.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ATL26241.1}.
FT DOMAIN 30..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1720..1795
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1813..2240
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3836..3911
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 459..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3995 AA; 416123 MW; CC134B8E773EACF1 CRC64;
MTNNDERLRD YLKRATADLR QARRRLSEYK EPIAIVSMAC RYPGGVRRPE DLWRVVSEGV
DAVGEFPEDR GWDVESLYDP DPEHEGTSYT RHGGFLADAA EFDAEFFGIS PREALATDPQ
QRLLLETAWE AFERAGLEPG SLRGSRTGVF AGVMYNDYGS RLFGRSPEGF EGYLVSGSAG
SVASGRVSYT FGLEGPAVSV DTACSSSLVA LHLAAQALRQ GECTLALAGG VTVMSTPSTF
VEFSRQKGLA ADGRCKPFAA AADGTGWGEG AGLLVLERLS DARKNGHPVL AVLRGTAVNQ
DGASSQLSAP NGPSQQRVIR QALANARLKP SEVDVVEAHG TGTTLGDPIE AQALLATYGQ
DRPAGRPLWL GSVKSNIGHT QAAAGVAGVI KMVMAMREGV LPKSLHVDAP SPHVDWEAGA
VSLLDEARPW EDNGHPRRAG VSSFGISGTN AHVIVEQAPE ASETDADAEA DAGDAEPTDA
AEQAVVAERG DLPELLALSA RTEGALRGQA ERLAAHLRAT PDVPLGDTAH ALATARTHFT
HRATVTARDH DEACAALDAL AAGAPHPRVA RGVTDASEGR TAWMLTGQGS QRPGMGRELH
AAHPVFARAF DEAVRHLDPH LDHPLRDVVF AEPGTPAAAL LDTTRYAQPA LFALQTALHA
LLTHHGAAPD VLIGHSIGEL TAAHLAGVLQ LPDAARLVAT RARLMQSAPT GGIMLAVAAA
PEEIAPHLEG QEHLVSIAAV NGPASTVVSG DAEAVRAIGR IFADQGAKTK ELAVSHAFHS
PHMEPVLDEF RAAAATVTYA APTVPVVSDV TGKLATTEQL TSPDYWTEHI RCPVLFHDGV
TALHADGVTR FLELGPDAVL TAAALETLRH LDGDADAGSG AGSAAVATLR SGHPEPESFT
TALGRLHTSG AAFALDRPGA ADARDTAAAL PTYAFERRRY WLAPAAGTAD LVTAGIDAAG
HPLLGAAVTL AADDSVLLTG RLSLATHPWL ADHAISGHPV LPGTALVELA LHAGEQVGCD
TLDDLTLQAP LVLPEQGAVQ LQLVLGAPDD GGRRALTCHA RPTDAQGADE EWTLLATGTL
VTGAPVITAE AAATADADPT TWPPAGARAE TVDGLYDRLA ALGYDYGPEF QNLTALWRAD
GGDDLYAEVR LPADAAESAD RFGIHPALLD AALHPLAAAL GTSDASVRLP FAWHGVRLAA
TGATTLRVRL TRTGDDAVAL NLTDHEGRRV AEVETLAVRP VAPDDLVRGR SAADDALFRV
EWTAVREPDE PVAETGAPEP WTTVTDTAEG AAPLPGVLFL TVGGAGTEDV PRSAYDVTGG
VLEQLQLLLS DERFDETRLV VVTRGALAVR DGEDIGDLAA APVWGLARTA QSEYPGRVTL
LDLGAGSGAG DVADAVRRAL TIGEPQLALR DGQFLAPRLA RAGVDAELVA AAPDPRGTVV
VTGASGTLGA RVARHLVTAH GARHLVLASR RGPAAEGAAE LVAELTGLGA TVSVVACDAA
EATAVDALFA GVDPAHPVTA VVHAAGVLDD AVLAGLTAEQ LRRVLAPKVA AAWNLHRATL
DLDLAAFVLF SSVAGTLGNA GQANYAAANT FLDALAQHRH ASGLPATSVA WGLWDESSGM
TGHLADADLA RVSRLGLAPL STEQGLALLD TALTAPHPLL VATRLDHAVL RAKATSGELP
ALFSGLVRAR ARRAVAAAAP GGGSAWAERL LALPAAERYG TALDLVRTAV AATLGHATPA
AIEADRAFKD LGFDSLMAVE LRNTLASLTG RRLSATLVFD HPSPAALARH LVEESVGSAA
PRAAVVVSAD TADDPIAIVS MACRYPGGVR RPEDLWRVVS EGVDAVGEFP EDRGWDVESL
YDPESGREGT SLTRHGGFLY DAAEFDAEFF GISPREALAT DPQQRLLLET AWEAFERAGI
DAAGLRGSRT GVFAGVMYND YGSRLSGRAP EGFEGYLGNG SAGSVASGRV SYTFGLEGPA
VSVDTACSSS LVALHLAAQA LRQGECTLAL AGGVTVMSTP LTFIEFSRQK ALSADGRCKP
FAAAADGTGW GEGVGLLVLE RLSDARKNGH PVLAVLRGTA TNQDGASNGL TAPNGPSQQR
VIRQALANAR LEPGDVDVVE AHGTGTTLGD PIEAQALIAT YGQDRPAERP LWLGSVKSNI
GHTQAAAGVA GVIKMVMAMR EGVLPKSLHV DAPSPHVDWE AGAVSLIDEA RPWEDNGRPR
RAGVSSFGVS GTNAHVIVEQ APEASETDTD ADPEPTDSAP VVPWILSAAD DASLREQAER
LREFLAEDES AGIRDVAYAL AKDRAALEHR AVVLGEDRDS LIAGLGALAD GEDSASVVTG
AATAIGGRTV FVFPGQGSQW PAMAASLYAT STPFREHIDA CADALAPYTD WSLRDLVTQA
PGAPGLDRVD VVQPALFAVM TSLARLWQAH GVQPDAVLGH SQGEIAAAYV AGALDLADAA
RIAALRSKAI TVLEGTGGMV SVPLAADATE ALIGPWRGDV QIAAVNGPGA TVVSGAADAL
DELLAHCSER EIRARRIPVS YASHHPHVEA LRETLFDQLA GITPKSAPIA FYSTVEAEPV
DTATLDADYW YRNLRHTVRF EETARRLVED GHTRFVETSP HPVLTVGLQD IIESTGTPAT
ATGTLRRDQG TAHRFLTSLA TVWTGGGPAD WPGTIPGGGA PHRRVDLPTY AFRRRRYWLE
PETTISDASG LGQHAADHPL LGAAVEVASG AGLLFTGRVS TTTHPWLLDH AVLDTVLLPG
TALLELALHA GGHVGADELA DLTLEAPLIL AAGASYDLQV AVDPADGTGA RAVHIHSREH
HDEPVAGEGW TRHATGVLAP GAAGQGAGFD LTAWPPPNAR PYPLNDVYER LARHGYVYGP
VFQGLKSAWR DGDDTYVEVR LPEDVRGEGE RFGLHPALLD AALHALALDG APAEGSDAAW
QVRLPFSWSG ARLYAAGASL LRVRLTRTGE DTVALRAADA SGAPVAAVEA LAVRPADLAE
LVASARTTGD DGLLHTEWVS AQLPADTGAD ASSGAVRGAL ALLGGHSAGL LRAAERPVTV
HESLLALQDG IEAGVPAPRA LLVTAVPAAN GLDSDIDTEE GPADTAQTIV PRFLGLLQSW
LADPRLAATT LVVATRDAVS TGAGDHVRHL AGASLWGLLR SAQSENPDRF LLIDLDGEPL
DAADLHAALD SGEPQLAVRK GEFLVPRLGR AATGHLLAAP SDDPHWRLAS KGTGSPDGLW
LAPAPDAARP LGEGEVRVEV RAAGINFRDI LIALGMVAND ARPPGGEGSG IVLETGPGVT
GIAPGDRVMG LLPEGVGPVT VADQRVLTRM PRGWTFAQAA GIPVVYLTAY YGLKDLAGVR
RGESLLLHAA TGGVGLATLQ LAEHWGLTVY GTASPGKWRV LRDRGLPDER VASSRDLDFE
DRFREATGGR GVDVVLNSLA QEYVDASLRL LAPGGRFIEM GKTDIREAAE VESAYPGIRY
QAFDVLDAGP ERVKEMLEEL RELFESGALA PLPSTAWDIR RAPEAFRFLS QARQIGKVVL
TLPAPPDPEG TVVVTGASGT LGARVARHLA AEHGARHLVL ASRRGPAADG AAELERDLTA
LGARVSVVAC DVADEAAVRA LFAGIDPTHP VTSVVHTAGV LDDAVLAGLT QEQVLRVMAP
KVAAAWHLHR ATLDLDLSSF VLFSSMAGTL GNPGQANYAA ANTFLDALAQ YRHASGLPAT
SLAWGLWAES SGMTGHLDDA DLARMSRLGL APISTEQGLD LYDRALAAAQ PVLLPVPLDL
PALRRQAADG SLPPLLSGLV RAPVRRAASA ADGTDAAAPD SLAADLAALP SAERPQRLLD
LVRRQVAAVL GLTGPEAVSA GKAFKQIGFD SLTAVELRNR LNAATGLRLP ATVVFDFPTP
TALAERLLGE LLPDGGPDTD VPADVTSVIA GLERLTATGA DVPDAATRDL LAARLREALE
ALGAAGSGSE PVGAVIDRAT DDEIFDFIDS ELGLS
//