ID A0A3N6GXW1_9ACTN Unreviewed; 2912 AA.
AC A0A3N6GXW1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dimodular nonribosomal peptide synthase {ECO:0000313|EMBL:RPK73262.1};
GN Name=dhbF5 {ECO:0000313|EMBL:RPK73262.1};
GN ORFNames=EES45_30405 {ECO:0000313|EMBL:RPK73262.1};
OS Streptomyces sp. ADI97-07.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1522762 {ECO:0000313|EMBL:RPK73262.1, ECO:0000313|Proteomes:UP000281409};
RN [1] {ECO:0000313|EMBL:RPK73262.1, ECO:0000313|Proteomes:UP000281409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ADI97-07 {ECO:0000313|EMBL:RPK73262.1,
RC ECO:0000313|Proteomes:UP000281409};
RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C.,
RA Busche T., Kalinowski J., Zotchev S.B.;
RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of
RT secondary metabolite biosynthesis gene clusters and some of their
RT products.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:RPK73262.1}.
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DR EMBL; RPGY01000149; RPK73262.1; -; Genomic_DNA.
DR Proteomes; UP000281409; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd17643; A_NRPS_Cytc1-like; 1.
DR CDD; cd05906; A_NRPS_TubE_like; 1.
DR CDD; cd19540; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000281409}.
FT DOMAIN 986..1063
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2782..2857
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1060..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2860..2912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2893..2912
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2912 AA; 312395 MW; 888FAA69859B5D16 CRC64;
MSLHEGPPRE DDHQPLSGAQ EGLWYAGRLA SDGAAHNTAE AVEIHGPLAT GLFETALRRT
VGEADTFAMR LLDTDDGPRC ERAPDAQDWV LRRIDVRDAD DPEAAAWQRV RADLATPVDL
DKGPLFSHTL LTLAPDRHLW LLTAHHILLD GYSYKLIGRR LADTYNALAA GAEPAPTVFA
PVSRLRTEEA AYLASERCER DRAYWSRRLA GLPEPARLTR RAHPPVAPFL RRTAELGSAD
VQALSDAATR LGATRTDLLT AAFAAYLHRM TGADDLVLGM ATMSRLGSAA LRTPGTASDV
LPLRVAAGAG TAVADLVRTV AGELTRLRRH QRYRSEFIRR DLNALGTGRR LYGPVLNIVP
FAESLDFGGS PATWHHLSGG AVDDLQVSVR PGPGPGGLWL AFDANPALYD EDELGLHRDR
FLALLRRLAE APPTTPVAGL ELLLPGEHPR HAPVRDLPVT ATLTELFERQ VRARPERVAV
THEGERLTYA QLDARANRLA RLLAERGAGP GRVVALALPR GLRLLPALLA VLKTGAAYLP
LDGGHPAERL RLVMDDVAPA LLVTETGLAR HLTGGVPAVV LDDPAVEADL AGRPAGGLTD
ADRRGPTSPS DIAYIIHTSG STGRPKGVPV VHAAVVRLFA AAAEHFDFGE DDVWTLFHSY
AFDFSVWEIW GALLHGGRLV VVPHAVSRSP HDFLRLLHRE GVTVLNQTPS AFEQLVEADG
EQPPGAGPDR TSTLRHVVLG GEALRPERLR PWADRHGLES PALVNMYGIT ETTVHVTHHR
VTPADLTDER RTGIIGRPLA DLRVHLLDPS GRPVPPGAVG EMYVAGAGVA TGYLGRPELT
AERFLDDPFG PPGCRMYRSG DLARRRADGT LEYLGRADQQ VQLRGFRVEP GEIEAVLAAH
PQVSRAAVVV RRADNGARQL VAYTVSAGQV PPDPAELRAH AATHLPDHMV PAVCVGVDAL
PLTANGKLDT DALPAPDFTA TAAGARPRTP RQALLCALYE DVLRLPRDTV GADANFFDLG
GDSLLATRLL ARLRHSTGAE VPISALFDGP TPAMLAQRLA DRPGTDPDRP GLGDVDRPES
VPLSHAQERM WVLHRLDDAA ATYNIPLIVP LGPLVDADAL QAALGDLVDR HESLRTVFAE
RDGAPRQRVL PPEESRPRLR RVDCPADEIA AHVAAASRHR FDLTGENPVA AWLFGAGEER
TLLLVLHHSA ADGWSLRPLA DDLSAAYAAR RAGRAPVRDP LPVQYADFAG WQRALLAPDP
DGAGRLERLT AHWRRALAGL PEACTVPGDR PRPASPRGDG AHVTEAVDTA LHRDLLHLAE
REGVSLFMVL HAAVSALLTR CGAGEDIVVG TPVAGRSEPA LDQLIGLLTN TLVLRADTSG
DPTFRELLAR VRPQDLAALD HQDLPFDRLV DELNPRRVPG RHPLFQVMLA LQNNEPAVLR
LEGHEVTLRP TATRTAKFDL FVDVLERHGD SGAGGLDLHI EYATELYDAA TAEEFARCLR
ELLRAVCADP DRRLGDLPAP PPRTPAAVRG PDAAEVTDTA LSVPGIRDAV ALAGSGGAPP
DLYVVPGRAD AAERVERILD EAGHGAVRVT AVNTLPRTDD GAVDAGALRA LPRVDAAAAD
SWRRHLAGLP GVRTAEVAVE AAPEELGRRH AGPPRRAAPP APAGRPGTTT AGTVPALSEG
PELTGPTVSG WAQALIRAAE RGHGDIVHVH ADGSETRRDY ASLVAEASRV LAGLRRAGLR
PGDRVILQCD ATEDFLAVLW GCVLGGLVAV PLTVPTSYAT PSAALTKLEG IWRMLGRPWT
VCSPALEAGL RDLAARQDWP GLRLTTADAL RDAPEDRDWY AARPDDLVLM LMTSGSTGLP
KAVRLTHRNV LTRSAATADL NGLGAEDVSL NWIPLDHVTG VVMFHLRDVY LGCRQVHAPT
TWILRDPRRW MDLAHRHRAT VTWAPNFAFG LLAEHADRFR DREWDLTPMR LVMNAGEVVV
AAAARRFLHT LKPFGLPQDV MHAGWGMSET CSVVTDAVLP AEPPGTDEAF VSCGLPYPGF
AMRIVDEHDT LLAEGDVGRL QVHGTSVTEG YHDNPAADAE AFTDDGWFDT GDLAFLRDGE
LYITGRAKDV IIVNGVNHYS HEIEACVEAL PYTVRSYTAA CAVRSGPTAT TDELALFVHL
APEHDPATAL REIAGKVTRE IGISPAFLVP VAADAIPKTE IGKIQRTKLR KSFEAGAFDD
AVREAQLLLG TAATLPDVFL RPVWQRAAPH LPRASAAGRH TLVLTGSDPR TQEISGHLAR
ALRADGGLCT EAIDGASYAR QNAARHYIRL TEEADHRALL RALDADGRPV DAIVHLGAPH
AADTEAPEAA ESGARSLLAL ARALADRPGG PHRTDLLYVT AGAQAITADD RPSPVHAMAG
AVLKSLREEL GGLRCVHLDL DPQGEEDPVP LLLADMTGTP ADTEVARRGG RRLVRRLAPL
PEPALPTDPP ASDGFHLLSG GLGGVGTEIA AHLLRTPGTR LLVLGRTPLP PEDTWPEHLA
AGGPPAARVE AYRRLRESGE VRYARADVTD ERQVREAVAA AAEHWGAPLV SVTHLAGALV
ERPVAQLDPA TWRTALDAKV RGALTLHRVS ADHPVGSFVT FSSVNGYFGG AMNTAYAAAN
AYLDALVLHR RALGLPGQSL AWSMWRERGM SSGYRLAPLT EARGYRVLDT ATALRSFDLA
RTLDEPHLLI GADRSVPWVR SHVLEPVRQV RRLAGRLALA EGTDLGALYR SAAHGTDGDH
WVLRAAGGGE RPTTTSEDEA GERLRALESR LAGLWRDVLG RDRVGPDENF FDLGGNSLLL
VAAQSVVNRE FGCELPVVEL FAHPTVRALA RHLASLTGPG AAGAPPAADP QAPPGTAGTG
PSGLDHAKER AQRQRAARAR RSARHGKDQG HA
//
