ID S5TUH8_9BACT Unreviewed; 2021 AA.
AC S5TUH8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:AGS49616.1};
DE EC=2.3.1.39 {ECO:0000313|EMBL:AGS49616.1};
DE Flags: Fragment;
OS uncultured bacterium esnapd12.
OC Bacteria; environmental samples.
OX NCBI_TaxID=1366592 {ECO:0000313|EMBL:AGS49616.1};
RN [1] {ECO:0000313|EMBL:AGS49616.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23824289; DOI=10.1073/pnas.1222159110;
RA Owen J.G., Reddy B.V., Ternei M.A., Charlop-Powers Z., Calle P.Y.,
RA Kim J.H., Brady S.F.;
RT "Mapping gene clusters within arrayed metagenomic libraries to expand the
RT structural diversity of biomedically relevant natural products.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11797-11802(2013).
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DR EMBL; KF264551; AGS49616.1; -; Genomic_DNA.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08952; KR_1_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 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; 3.40.50.720; 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; 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; 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; 2.
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; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
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; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:AGS49616.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGS49616.1}.
FT DOMAIN 434..509
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 527..951
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1909..1984
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 506..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2021
FT /evidence="ECO:0000313|EMBL:AGS49616.1"
SQ SEQUENCE 2021 AA; 211690 MW; 6CD360041D0A621A CRC64;
MRAHLDQLGG QGADVHRVDI DRVGAALAHQ ETTQPGAHRA VVVAASTAEL LDGLTALADG
QPHNSVIRGV AAPAAPVVFV FPGQGAQWPG MATDLLSDSA VFRAAMDTCA RAFESVADWS
LSSVLNSAEQ LRRVEVVQPA LFAVQTSLAA LWRSFGVPPD AVVGHSIGEL AGAHVCGAAD
AAAAARAAAL WSREMIPLVG NGDMAAVALS VEEISPRLAK WDHDVTLAGV NGPRSVLLTG
SPEPIAGCVA ELSAEGIRAQ VINVSMAAHS AQVDDIADRM RSALAWFAPV SSEVPFYASL
TGGQLNTAEL GPDHWPHSFR SPVRFDEAVR SVLDISPGTF IEVSPHPVLA AALQQTLDVA
RSSATVVPTL HRRQSGMRQF LLAAAHVFAG GVTIDWTAAY DDVAPDPGAL PQGAAPVEHQ
DEQPAGFDWN APAQVLHDRL LSIVNSQTAA LTGSDVDAQA TFRELGLDSV LVAQLRTKLS
AMIGVDVNIA LFYDHATPRA LAEALARPSN DPTPDAIHAR TKGPKPDEPI AVVAMACRLP
GGISSPEDFW ELLSEGRDAV AGLPTDRGWD LDSLFHPDST RSGTAHQRAG GFLHGATTFD
AAFFGMSPRE ALAVDPQQRI MLELSWEVLE RAGIAPTSLH ASPTGVFIGL IPQEYGPRLA
EGGDGVEGYL MTGTTTSVAS GRIAYTLGLH GPAISVDTAC SSSLVAVHLA CQSLQRGESE
LAMAGGVTVM PTPGMLVDFS RMNALAPDGR CKAFSADADG FGMAEGAGML LLERLSDARR
NGHPVLAVIR GTAVNSDGAS NGLSAPNGRA QVQVIHQALA EAGLKSSEID AVEAHGTGTR
LGDPVEAGAL LETYGRGREQ PLWLGSVKSN LGHTQAAAGV AGVIKMVLAM HAGVLPPTLH
AGQPSTEIDW SSGSISLLNE RVPWPSGERI RRVGVSSFGI SGTNAHVIVE EAPRPTAGER
TPSGGAAPWV LSASSADALR AQAARLAAHL REHPGQDPRD VACSLATGRA ALRHRAAFLP
TDASAALRTL DQLAAGTPDG VSVGASRPDH GAVFVFPGQG WQWAGMAVDL LDTSPVFAAA
LRECADALTP HLEFELIDFL RAEAEHRECD TMLSTDRVDV VQPALFAVMV SLAALWRSYG
VEPVAVLGHS QGEIAAACVA GAITLDDAAR VVARRSRVLE RLPGHGGMAS IAAPVDEVTR
RLGEHLEIAA VNSPRSVVVA GARDELDTLI ASCLADGVRA TRLAVDYASH SSHVEAIRDA
LHSELGDNFS PLPGFVPFYS TVTGRWTEPG ELDAGYWYRN LRQTVRFDDA VRGLIAHGHR
TFLEISAHPV LTGAIEEIGE DTGVELTAIG SLRRGDGTIG HFGEALCRAF VAGVTVDWQS
VHVGTGARRV PLPTYPFQRE RFWWEPRPML PESVESEEIS ALRYRIEWRP IVADESVRLD
GTWLVASYAG TADDMCAAAR EALQAAGAAV NELVIEPRTT RDELTQRLRC AGDVAGVLSL
LAVDEDEAHG QPLALTSLAD TLSLTQALGA ADLECPLWVI TENAVAVDPV EGVGNPAHSA
LWGLGRVVGL EIPAGWGGLI DVPAGSATAL SRHLAAILAG RTGEDQIALR PAGAHARRWV
RATASSTPVR QWKPSGTVLV TGGTGGVGKH IARWLAQRGA PHVLLVSRSG PEAAGANELA
AELNALGAQA TLAACDITDR EAVRALLSSI DDELPLSAVF HAAATLDDGT IETLSGERIE
RANRAKVLGA RNLHELTRDM DLSAFVLFSS FASAFGAPGL GSYAPGNSYL DGLAQQRRRD
GLPATSVAWG TWAGSGMAEG PVADRFRRHG VIEMPPARAV QALQTALDRS EVCPIIIDIQ
WDRFLLAYTA QRPTTLFDEL GAGGAAAAPV VAERQTDTLA ALPAPEREKA LIELVRSHAA
AVLGHASAER MPTDQAFAEL GVDSLAALDL RNRLAAATGV RLPTTTVFDH PNVRMLAAHL
AAELAGAASV EQALSVGGVG VDGDDPVVVV GMACRLPGGV G
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