ID A0A0N0N6L5_9ACTN Unreviewed; 1942 AA.
AC A0A0N0N6L5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=6-deoxyerythronolide-B synthase, (Acyl-carrier-protein) S-acetyltransferase {ECO:0000313|EMBL:KPI21988.1};
DE EC=2.3.1.38 {ECO:0000313|EMBL:KPI21988.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:KPI21988.1};
DE Flags: Fragment;
GN ORFNames=OK074_7262 {ECO:0000313|EMBL:KPI21988.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI21988.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI21988.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI21988.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI21988.1}.
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DR EMBL; LJCV01000026; KPI21988.1; -; Genomic_DNA.
DR SMR; A0A0N0N6L5; -.
DR PATRIC; fig|1592327.3.peg.1005; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047879; F:erythronolide synthase 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:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; 1.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KPI21988.1};
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:UP000037991};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPI21988.1}.
FT DOMAIN 1..176
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1748..1823
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 179..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1825..1845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1889..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPI21988.1"
SQ SEQUENCE 1942 AA; 201245 MW; F7776294D3020C8C CRC64;
GAARRPGLAV VAGSAVNQDG ASNGLTAPNG PSQQRVIRQA LASAGLTAAD VDAVEAHGTG
TSLGDPIEAQ ALLATYGQDR PEERPLLLGS VKSNIGHTQA AAGVAGVIKM VLAMQHGLLP
RTLHANEASS HVEWSAGAVD LLTDNADWPR TEERARRAGV SSFGLSGTNA HVVLEEAPLQ
GQPESVAPST GSAGGPATGS VGSAGGAVPW VVSGRTAAAL RAQAEQLAEF VAGDVTLNVA
EVAGSLVRSR SLFEHRAVVW GADRAELLEA LEAVASGAES ANATAGTARR DTRTAFLFAG
QGSQRLGMGR ELYETYPVYA DAFDAACAHL DAELPRPLRE VVFGDDVELL NRTEFTQPAL
FALEVALFRL LESWGVRPDV LAGHSIGEIA AAHVAGVWSL ADACRLVVAR GRLMQALPTG
GAMVAVQAAE DEVLPLLNDR VGIAAVNGPQ AVVISGAADA AEEIAAHFRA QDRKTTTLRV
SHAFHSPLME PMLAEFRAVA EQLTYERPQL AVVSTVTGEA VAADELTSPE YWVRHVRATV
RYADAVRALA EENVTRYLEL GADGTLTALA QATLDAPEAA VLVPVLRKDR PEAGALLAAV
ARLHVDGLPV DWTAQLPSSE PVVLPTYAFQ RRRYWPNFTG VTLGDLGSAG VGSAEHPLLG
AAVRVAGSEE ALFTGRLSLK THPWLRDHAV TGTVLFPGTG FLELALCAAG QLGYDRVEEL
TIAAPLVVPE RTGRLVQVRA GAPDESDART VEVYSRAEDA LDTDPWTLNA TGSLTTTTPV
TTTPDLSAWP PPNAEAVPTE GFYDRFAEAG FAYGPVFQGL RAVWRRGDEV FAEVGLPDDH
ERLAGGFGVH PALLDSALHA MMFVSLADAG QGRLPFSWSG VSLRASGARS LRVRMVQAGP
EAVALHLADP TGGTVASVES LLLRQVSGDL AARAAAEGHR DGLFQLDWPK LTTSAGQHGF
GYGEVAVVGD DTDLAPGVPV HPTLAELPAV VPAHVLFAAT TGHGSGTPLT DSTRSAVGRV
LDAVRTWLAD ERYEDARLVV VTEGAVALDE TAPDPAGAAV WGLVRAARAE APDRFALVDT
DGTDASRAAL AQTLASALAA GEPEFVLRDG VAHAPRLGRV PAGGQLPLPA DESAWHLDSI
EKGTLDNLAL TPFPEAAAEL TAGQVRIAVR AAGVNFRDVL NALGMYPGEA GLLGGEGAGV
VTEIGPDVTE LAVGDRVMGM FPGSFGPVAV ADARTLARIP VGWSFAQAAS VPIVFLTAYY
ALTDLGGVRA GESVLVHAAA GGVGMAATQL ARHLGAEVFG TASAGKWGTL RELGLDGAHM
ASSRDTAFEA AFLAATGGRG MDVVLDSLAG EFVDASLRLL PRGGRFLEMG KTDVRDPDTV
AAQHADVMYR AFDLWEAGPE RIGEMLADLV ELFNSGVLQP LPVTCWDVRR APEAFRYLSQ
ARHVGKVVLT VPAPLDPDGT VLVTGGTGGL GALVARHLVT EHGVRHLLLA SRRGLDAPGA
RELVAEMAEL GATADVAAVD VADRDQLAAA LHTPPPPHPL TAVIHTAGIV DDGVIGSLTS
ERLAAVLRPK ADAALQLHEL TRDMDLAAFV VFSSVAGTFG SAGQANYGAA NAFLDAFAAT
RRAAGLPAVS LAWGAWAPGA GMTADLTEAD LRRMARGGMR TLSAEQGLQL LDTAGLLTGA
APAHRAALLP VNLDLQALRA HADAVPPLLR GLVRAPARRA AETAGGGGAE RQDLGATLAG
RAPADREQFL VDLVCAQAAA TLGHASADEI EPDQAFKELG FDSLTAVELR NRLNAVTKLR
LPATLVFDHP TPTALAGQLL TEIALPEADG PDGPNGPGTA QGTSAGTAVT AAPLLVELDR
LEAALAAATV GGDDHVTITS RLQRLTAKWQ EQATKGGAGH DTGTGSGDPG TALTDADDDG
ELDSVATADE LFDLIDKELG MS
//
