ID D7BSM2_STRBB Unreviewed; 2188 AA.
AC D7BSM2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Modular polyketide synthase {ECO:0000313|EMBL:ADI11519.1};
GN Name=nanA11 {ECO:0000313|EMBL:ADI11519.1};
GN OrderedLocusNames=SBI_08401 {ECO:0000313|EMBL:ADI11519.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI11519.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI11519.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI11519.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP002047; ADI11519.1; -; Genomic_DNA.
DR RefSeq; WP_014180969.1; NC_016582.1.
DR STRING; 749414.SBI_08401; -.
DR KEGG; sbh:SBI_08401; -.
DR PATRIC; fig|749414.3.peg.8645; -.
DR eggNOG; COG0604; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_2_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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; 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; 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; 1.
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; 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; 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; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000000377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2004..2079
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2081..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2139..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2084..2107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2153..2167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2188 AA; 229455 MW; 98E825CEEBAFEEE1 CRC64;
MANQEQLVDY LKRVATDLHD TQQRLREVEA RDRQPIAIVG MACRFPGGTD TPEALWDLVS
EGRDVISPMP DDRGWDPGMF NDSGETGTSY VREGGFVHDI ADFDADFFDI NPREALAMDP
QQRLLLETSW EAIERARIDL TSLRGSKTGV FVGGSTVYYA GNAAGVPQDV AGYLATGLAA
SSMSGRISYT FGFEGPSFTV DTACSSSGVA LHLAVQALRK GECSLALAGG VCVMATPGTY
LEFSKLNGLA ADGRCKAFAA AADGFGPAEG VGVLLVERLA DAERLGHPVL AVIRGSAINQ
DGASNGLTAP HGPAQERVIR AALADAQLSA RDIDVVEAHG TGTSLGDPIE AQALIAAYGR
RRADGGPLWL GSVKSNIGHT QAAAGMAGVI KMVHALRHGL LPRTLHVDEP THQVDWSEGT
VRLLTEARPW PEAGGPRRAG VSSFGMSGTN THVILEQAPP AEEPAPAAES PVVPWLVSGR
GEAALRAQAA RLRDFLAERP EASPTRVGFA LAGSRAAQSH RAAVVAADRD TLLAGLGSLA
EGTPAGHVVT GSVSPGATAF VFPGQGSQWV GMALALADAS PVFAEHFRRC AEAVERHTGY
TVESVLRADP GAPSLDRVDV VQPVLWAVMV ALAELWRSYG VEPAAVVGHS QGEIAAACVA
GVLSVDDAAR VVVLRSQVLP ELSGRGGMAS VAQPVELVEK HLERWDGRLS VAAVNGPSST
VVSGDADALE ELLEGYEADG VRARRVPVDY ASHCAHVDAL RGPLLDALSG IEPKAGTVPL
YSTVTGRRID GTTMDAGYWY TNLRQQVRFQ EATEALLADG HGVFIECSPH PVLTIGVQET
MDQSGANATA LGTLRRDEGG WDRFLLALGQ AHAHGVAVDW SRVFPDGTSP ADLPTYAFQR
RRYWLDATAG AAGDPASLGL APADHPLLGA VTLLAEGDEV VMTGRLGLDT HPWLADHAVA
GAVLVPGAVF VELAVRAGDE VGCDRLEEMV LASPLVLPEQ GGFDLQLVVG GADEDGRRTL
GVYARPSGSD RPWVQHVTGT LAPGGAARPF DLAQWPPEGA RPVPVEGCYD QLAEGGFRYG
PAFRSLRAVY RRETEVFAEV VLPEEQRGKA AAFGIHPALL DGALHASGLS AVRGDSEGRM
ALPFAWNGVS LAATGAELLR VRLAPVGDDG MSVHATDASG HPVISIESLV TRPFTAGQLP
SGGGDETRDG LFRVAYTPLT DPEPGTATDD WTAVATGSEP TCYGVRRYGD LDALAAAVDG
GLPAPPVTLL PCEPAPDDGD LPGALRRRLG EVLHTVQRWL ADERFAVSRL VVVTRGAVAA
FEGDDVTDLV HAPVWGLIRS AQSEHPDRLV LVDLDGPELP KAVAAAVAVA VAAGEKQIVV
RDGTVRVSRL VPAVSGGALA LPETPHWRLD IAAPATLDNL GLVAAEEPGP PAPGHVRVQV
RAAGVNFRDV LIALGMYPGD GAFRGSEGAG VVLEVAEDVT SVAVGDRVMG MFQGAFGSTA
VADARSVVPI PPDWTDEQAA AVPIAYVTAW YGLVDLAGLK AGESVLIHAA TGGVGTAAVQ
IARHLGAEVY ATAGPGKHHV LEAMGIDEAH RASSRDLDFE DAFRAATGGR GVDVVLNSLT
GDHTDASLRL LAEKGRFVEL GMTDVRDPEQ LAEPYPGLRY RVLDLREPGE DGIGRMLTEI
LGRFARGELT HPAVRAFDIR RARDAFRLMS RAAHIGKIVL TLPRPLDPDG TVLVTGGTGT
LGGLIARHLV TRHGVRHLLL TSRRGPEAPG APALREDLAA LGATVTVTAC DAGDRERLAE
VLAGVPDAHP LTGVVHCAGV LDDGMVDALT PEQLARVLRP KAEAALHLHE LTQDADLALF
VLFSSIVGVY GNPSQANYAA ASTFLDALAQ HRQAGGLPAQ SLAWGMWEET SALTGELDDG
ARQRISQAGM DPLPTEQALA LFDRSYAVGD ALLVPIRQST AASRGGLAAG RTRARRVADS
GVAGTGGPSL TDRVTALPEA ERDSCVLEAV RAHMAAVLGH DSADEIAPDR TFKELGFDSL
TAVELRNRLS AATGLRLPAT FVFDFANPVA LAEHLREQIA PPTELGPPTD PSTPADPSPP
PGLPEGPSTD PRESRVRQVL AAIPLRRLEE SGLLETLLRL GEGPGEADTT GARPVEGTRD
ETHTPDSTDI ASMDLEELVN AALRNDES
//