ID A0A2A4KSX5_9ACTN Unreviewed; 4224 AA.
AC A0A2A4KSX5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:PCG87385.1};
GN ORFNames=CIB93_04210 {ECO:0000313|EMBL:PCG87385.1};
OS Streptomyces sp. WZ.A104.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2023771 {ECO:0000313|EMBL:PCG87385.1, ECO:0000313|Proteomes:UP000217525};
RN [1] {ECO:0000313|EMBL:PCG87385.1, ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|EMBL:PCG87385.1,
RC ECO:0000313|Proteomes:UP000217525};
RA Xu L., He S., Yan X.;
RT "Isolation and Genomic Analysis of a Bioactive Actinomycete Associated with
RT Cyanobacterium Lyngbya cf. aestuarii.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|Proteomes:UP000217525};
RA Jiao Y., Han B.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:PCG87385.1}.
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DR EMBL; NWVL01000005; PCG87385.1; -; Genomic_DNA.
DR OrthoDB; 5478077at2; -.
DR Proteomes; UP000217525; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; cd05930; A_NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
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; 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; 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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 3.
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; 3.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 3.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000217525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 588..665
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 701..1125
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2159..2233
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3233..3308
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 565..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1835..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2112..2157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2232..2253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3813..3844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4224 AA; 438526 MW; 5AE4BF42CEBAEF30 CRC64;
MTLLDVLLGA AREAPGQVVV HVCGDGSELT VTLRELLDDA LRVAGGLREA GVAPGTCVPL
LADRSEDFQP MFWGALAAGL VPVPLAPDVR RVLPVWEHLG RPPVVVDAAN APLARELPCG
VRALSLDVLR EGPELPEPAT GNAGQDEVAF VQFSSGSTGT PKGVEVTHGA VLANLEQIRG
ASTLGAEDVV VSWMPYFHDM GLIGTHLAPL AARAKQVKIG PLSFAKRPRV WFETADRHRA
TVLSAANFAL ALAVRRVPDE VVEGLDLSGV RLILVGAEPI APAVWRDFAR KMRPAGLDPA
ASQPVYGLAE ATLAVTFPPP GEVAEPLVLD RAALSVGEAV DAEPGPEAVE FMDVGVPVAG
CNVRIVDDAD SVLGDRRVGH IMVSGPQLAR GYQSLPEVSA EAFADGWLRT GDLGFLRDGR
LCVTGRHKDV LFLNGRTFHA PDMEEIAAET PGLPAGAPAV IGSTDPVSGG ERVVVFVPWA
RPPHDASDVL ERVAARVREA LLHDDVRVLA LPPGAFPRTT SGKLQRQRLR ERFEAGAWGA
GGPGAAAVSS VPSAASMASV RMEAGSSRAA ASPRARTETP TSRAEAPLPR AQAEAVVRDV
WARVLELPAP AVGRDERFGS LGGTSLKAME VLVALEEAFG VTLPPAVIRD HGTVAELAAH
LLTVAPGSRA GERESRAEGD AVPPRVMEGD NNGAGPHGSP VPATAVIGMA CRFPGADTPD
AFWDLLTGGH DAVTSVPEGR WDAAGQRGAT PDGPDGQRRR QRWGAFLDDT AGFDAAYFGI
GDDEARALDP QARLFLELSH EALERAGYAG PRRRGRSIGI FAAVGDSGYR AVLDRASADG
SPLPASLTGN LPNLIAARVS QSLDLDGPAL AVDTACSSGL VALHLARRSL LDGECDLAVV
GGVNLHLTST GHRLLEEAQA LSPTGRSRAF SADADGFVPG EGGAALALTR LDAARLGDDP
VLAVVRATAV NNDGRSLSLM APNPLRQREV ITRAYQEAGV DPASVTYVEA HGTGTAVGDP
IELRSLAHAF PVRPGGEPRL LGSVKTNIGH LLNAAALPAL VKVVLALGHR RLPPSLHHTP
PSPGLAPAGF SVVTEARDWT SAGPLVAGIN AFGFGGTNAH AVLEQAPPPP TRAGLGRTDA
GPHLLTLSAR SAAGLREAAS QLADHLDRHP QLGEGDVCRT ASTSRDDGPY RLALVADEDL
RDLRDRLADA SAASAASAAS AASAASAAGS LARSRPRVVF LFPGQGAHFP DRGGALYRTA
PVFRDTLDEA SALLGPVRGR PLLDWGLNPD REVEALAAMT EVAQPLLVAS GVALARQLRS
WGVEADAVAG HSVGEIAAAC ASGALSLADA VRFAAERGRL MGEFTEHGAM LAVRGGEEAV
ASVVAESGGA LVVAAYNGPG LLVLSGDVPA VESAARDLDA QGVPVRRLSV SRAFHSPLMR
PIAERLADAA RKLTPHTPST PLMSTVTGAW QPVLDPDYLR EHALRPVRFG AAVQRMTSEG
YDTFVELGRG GTLLGPVRAA SRGGGGGCSG ASGASGASGA SGASGASGAS GASGSDRAAG
SDRGGSGGRG RVVMLSALSA DSDSRSSSAS APGDGRLGRG ALLETVGRLW SSGVPLDRTA
LDADRRLVPL PTYPFQRTRY WADPPTSPLL HRVQWQDTPL PGPPAAVRSV LLTGPDTASV
NALSAQLAAE DIQVYGSADG QPDAVVLVAG PAPEQHDGET LNRAQDAALA AFDTALAHLD
ETGASRLLVL TEDVHTTGAA PERPRPAHAL LTGLLLAVPQ ETPGSSAIGV DLCSLDTPAL
RLEAVLAELR ADGAPGEAGT IAWRAGRRLT RAVPPLADAD VPPPGDSSTS TGSAPSSLTP
GSTTLPPDGT FLITGGGGGI GAALARDLAS KGRPTLVLAG RSPGLPTGLT EELRALGATV
RYHMADVSRE PDVDALIAAL PHLDAVFHAA GVVRPGTLRS RTREEAAEAL AAKTRGSLLL
SLALRRHGLR PAVCVAFSSV SAVLPGLAGA LGDYAGANAF LDAFAAAERA SGRPWQSVNL
AAFAETGMTA GLSTGTGAGA RAVPGTSPGA HASLVSRPGG RPVATAPALA ALRTAWGVDA
AQLVLADLAP SSAYSSPPAG RQERPAGTVP VRGTAPGFVP DAQPWPSPTA REGTTGSGTD
TAALLRRLLA AALRLSPAEI PDDEPFLTLG LDSLAAVDLV RQLERERGTA LPATLFFEYR
TVRELAAHLD APSPASPCAS GHGPASGRDP VPEGVPFPLT PVQLALHTSS RLHPDVPAHG
YVRQTVRGPL DTGLLGRALA LLADRHSMLR IRIESATDGR STDGRGTTRP QQYVAPAVDV
TAWYAVRDGL DGRVEELETA LCNRPFDLAA EPPVRAVLVR ESSELAHLLL VIHHAVGDGY
SLNILGEELW SLYTSLAHGD EPALPAPGTD FAGYASAAAE ERASSAGAAA LDSDRRYWAH
RLASRSEAPR LPLPYDGDPA ALPAPPLTTH QSALDSVLTG TLEERAAAHG VSLFHLLLAV
HVRCLARWSG QREIAVNVAR ARRDVRLAGV DRLVGPLADT LPLLCDTDPD ESVWTLAERL
GRVWLESEQH AAPTSLDLAR LLPAGLTGDG LRTVSPAGFS FARFPAALDE RCPVTVRPAA
AGTGTPATRL SLLCWQDGTI LRFSWNFPAR LFDPATVARL DRDFHDELTA AAGTLSDSGT
GSSATIVRRL LDRFRATPDA VAVDTGTGSG ALTYAELDQA SRSVAARLVA HGVTPGSLVG
LLTEPGADTV VSVVAILRAG AGWVPLDAGH PTARLADQIA RTGVRTVLCH APTRAAGDAL
RDVTQVPVDV PAPECAQGSE QGQDNVRELP EGAVDAESIA YVIFTSGSTG RPKAVPITYR
SMENYLDWAI GTFGYDAHDR LAQTASICFD ASVRQLLAPL LVGATVVAVP WNLLRDPSLL
LTHVERTRIT VWSSVPTLWE QLLTAAEERI RSGGPRPDLG ALRWVHVGGE ALPPAHVRRW
FDLLGDGQRI ANLYGPTEAT INTTCHIISA RPGDDVRRLP IGRPVAGTEV EVVGPDGRTL
GPGEAGELLI AGIGLTSGYL GEPDLTEAAF TTRRGRRWYR SGDRVRWSAD GGLEFLGRLD
DQVKVRGHRI EPGEIEAVLQ THEDVTHAVV LLQDGRLTAF VTPRPGTSGA DAVELRLHLG
KTLPPYLVPS RITSVDSLPL TGTGKIDRRQ LLALRAAAVS DSAGPAETPR RTPPRTPTEI
RLARIWSELL GTGDVCREDD FFALGGDSLL VLEVFARLEG TGGPLPRPTV IYRHRTLAAL
ATAVDNGAPA TPGTETDAGT GTDTGTRMDA GTGMAGVGEL SYAGPGPGPS PFPLTPTQRG
FLLAEAIAPG STSSWLTRLR LLGPLDTARF QSAVDALVAR HPMLRTVFPA GARPAVQQEL
PPSLRLPVEF ETLSEPHHLD ERIDSERARR FELWAWPLLR LRVFTLAPDE HVLVVHAHHI
IGDGYSAALL VRELMAVYDA SAEGEQPVLA PLRGTFRDYA VRAAVPADST GTPGGTNAAG
ATGDRAGDGG ARWARLSAPY PCPVLRPVLG SGNGPTGKEG EAEVVVPGGL RPAFHAHSFV
VDAGHVTELR GLASRVGTTL HAPVLTAYYR ALVAATGRAD LVLGLAVSGR DHSAQPDVHR
VFGPYATAVP LRPAAGTEAE SGRPAEAAFE DDLRRIAAEA TAARTHEGPV PSLPNGLPLA
SQFFFTYLDF SALGPESGQT LRVIQEDGDS VYTPPPVGTD VFLSARLDAG RLRLTVRAAA
AAFTPEGLAA FAETVRENLT HAAASSASVH ASAGVQGRAL GRPSGTGTGP APGPGTGPGP
DQQRMDAALV GYLPSPGQLA RLAGLSEEAL PREELRTLLF PGGRPRLLET LSTPLGRSGF
VCVPLFADEL APGDSLLGHT ARGVDLASSL GARSVSLAGM IPSLTGYGFD VLRATGTTGA
AVTTGHAATV VSVVKTVHAA LDARQQELSD VTVAFVGLGS IGSSSLELLL GLAGRPPARL
LLCDVRGSGP RLEELARSLR ERGLAGAVDV IDSDRGLPGE VYGARLIVAA VSGGGTLLDV
DRLEPGTTVI DDSFPHCFDT HRAIGRMGRS KDVLVAGGGL LTVGATERHV ADGLPAAAAS
GYAAQPWLPG TIASCRLESL LHSSEAGVPL VRGPVDSTTA LAYWAAAEAT GTRAAPLHLL
THAIDVDSLV PWAGKAVAPG GGSR
//
