ID A0A0N0MW65_9ACTN Unreviewed; 2153 AA.
AC A0A0N0MW65;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:KPI09848.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:KPI09848.1};
DE Flags: Fragment;
GN ORFNames=OK074_9127 {ECO:0000313|EMBL:KPI09848.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI09848.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI09848.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI09848.1,
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:KPI09848.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJCV01000239; KPI09848.1; -; Genomic_DNA.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase 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; cd08956; KR_3_FAS_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; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 3.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
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; 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; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 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; 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; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KPI09848.1};
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:KPI09848.1}.
FT DOMAIN 1101..1176
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1198..1624
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1065..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2153
FT /evidence="ECO:0000313|EMBL:KPI09848.1"
SQ SEQUENCE 2153 AA; 223563 MW; 81A57E3757595CB9 CRC64;
MGLELAAAFP VFADALDAVC AVVDPLLGRS LREVLTEESG VLDRTGLTQP ALFAVEVALF
RLVESLGVRP DVLIGHSVGE LAAAHLAGVL SLEDASRLVV ARGRLMEALP SGGVMVAVQA
SEAEVLPLLT DPRVSLAAVN GPEAVVIAGA EDAVQAVVEQ LPGRVRRLRV SHAFHSPLME
PMLAEFREVA ESVRYGVPRI PVVSNVSGRI AEGDELSSPG YWVEHVRRPV RFLDGIRTLS
DLGVSRILEL GPGGVLTAMA RECLPPDNGM LLVPSLRKDR PEPESMVAAL AGLFTDGVDV
DWSPLVAGGR VTPLPTYAFQ HQRYWLEPRG KAVGASDLGL TAADHPLLGA AVGLAGGGGV
VLTGRLSLKD HAWLVDGVVH GRVVVSGGTF LELALRAGDE VGCGLVAELV VDSPLVVPEQ
GAVHLQLVVA GPDDADRRAF TVHSRAADVS SDAPWHQHAH GVLAAAVGPV PDDAPVPDDA
PDLDDAPDLT VWPPAGADAS DADGVWRRDG GVFAEIALPT DTNTDDVTAY GLHPALLEAV
VRAIADDQQS QGQPLVISGL RGARLLASGA TALRVHLSAT GALTLADHTG APIACADEMR
TTVLTSDDLP APAHADALFQ VAWVPVPLPA AQSPAGRFAV LGADPLGLAG QLPASASDPD
TVLASFVSDF SNTTEGADGS TGVDADAAAE AAHRALATVQ SWLADDDRSV GVRLVVVTRG
AVAARDGEEV ADLTHAPVWG LLRSAQSEHP DRFVLVDLDG SRASLAALPA ALATGEPQIA
VRAGRAYAPR LARTDPSRST AGTVPFVPGD GTVLVTGATG GLGRLVARHL ADVHGVRRLL
LVSRRGAEAP GAADLRAELA ALGAEVTYAA CDVADRTALA AVLAAIPAGW PLTAVVHVAG
VTDDAVTETL TDAQLDRVLR AKVHAAANLH ELTDGLDLSA FVLFSAAAGL LGGPGQANYA
AANAFLDALA HRRRATGLPA VSLAWGLWAE TGGMGGRLSE TDVRRMARGG VLPLSAEQGL
ELLDTALGID EPLLVPIRLD TTVRPDTTAH EVPALLRGLV RAPVRRAAQQ PRTADAGGSG
SDSGKSYAER LAELPVVERG RVLLELVRSQ AAAVLGHADA GAVGAEQAFR EIGFDSLTAV
ELRNQLNTVT GLRLSATLVF DYPTPDALAR HLNTELLGED EDGRADDRTP VRTAAAVDEP
IAIVGMSCRF PGGVASPDDL WRLLRAGEHA VSEFPSDRGW DVEDLYDPDP DRPGKTYVRQ
GAFLRDVGAF DAGFFGISPR EALAMDPQQR LLLEATWEAF ENAGIDPASL RGSQTGVFAG
TNGLHYTSRV TKVPQNVAGY LVTGNSASVV SGRISYTFGL EGPAVTVDTA CSSSLVALHL
ASQALRQGEC TLALASGVTV MSTPGFFLEF SRQRGLAADG RCKAFSAEAD GMGASEGVGV
LVLERLSDAR RNGHEILAVV RGSAVNQDGA SNGLTAPNGP SQERVIRQAL VNAGVSAVEV
DVVEAHGTGT RLGDPIEAQA LLATYGQGRS EERPLWLGSV KSNIGHTQAA AGVAGVMKMV
LALQHGVLPR TLHVDEPSGQ VDWSVGAVSL LTEEQAWEAD GHPRRAGVSS FGISGTNAHV
IVEQAPDPVV EEPSVQGPVS PVVPLVVSAR GEGALREVAG RLVPVVGDGG VGVVDAAFSL
VSGRAVLGHR AVVWGRDRGE LTSGLEAVHR GERGAGAVVG VASSGGRLGF AFTGQGAQRP
GMGLELAAAF PVFADALDEV ASVVDPLLGR SLRGVLAEES GVLDRTGVTQ PALFAVEVAL
FRLVESLGVR PDVLIGHSVG ELAAAHVAGV LSLEDASRLV VARGRLMEAL PSGGVMVAVQ
TSEQEVLPLL TDPRVSLAAV NGPEAVVIAG AEDAVQAVVE QLTGRVRRLR VSHAFHSPLM
EPMLAEFREV AESVRYGVPR IPVVSNVSGR IAESGELSSP EYWVEHVRRP VRFLDGIRTL
TDLGVSRILE LGPGGVLTAM ARECLPPDNN TLLLPSLRKD RPEPESMLAA LAGLFTDGVD
VDWSPLVAGG RVTPLPTYAF QRQRFWLEES SEGSGGWGLG PAVVLADGEG VVFSGGVSLR
THGWLCGHVV HGRVVVPGSA FVELVLRVGD VVGCGTVAEL SVDNPLAVPE RGG
//
