ID A0A498E0M2_9ACTN Unreviewed; 3270 AA.
AC A0A498E0M2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:RLL69343.1};
GN ORFNames=D7M15_23725 {ECO:0000313|EMBL:RLL69343.1};
OS Streptomyces sp. Z26.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2500177 {ECO:0000313|EMBL:RLL69343.1, ECO:0000313|Proteomes:UP000288048};
RN [1] {ECO:0000313|EMBL:RLL69343.1, ECO:0000313|Proteomes:UP000288048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z26 {ECO:0000313|EMBL:RLL69343.1,
RC ECO:0000313|Proteomes:UP000288048};
RA Buchmann A., Cano-Prieto C., Baz M., Hassani L., Barakate M., Nafis A.,
RA Niedermeyer T.H.J., Gross H.;
RT "Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces
RT sp. Z26, isolated from potato rhizosphere in Morocco.";
RL Submitted (OCT-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:RLL69343.1}.
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DR EMBL; RCHV01000002; RLL69343.1; -; Genomic_DNA.
DR OrthoDB; 9030879at2; -.
DR Proteomes; UP000288048; 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:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
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; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
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; 2.
DR Pfam; PF00668; Condensation; 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; PF00550; PP-binding; 3.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000288048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 548..625
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1635..1709
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1739..2147
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2888..2963
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1611..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2320..2339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2857..2890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3251..3270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2870..2885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3270 AA; 340943 MW; 9B9B2238212289DE CRC64;
MRTPATPVPS TPSVPATAPG LARAVYEQSR RTPHAPAVRD GARTLDHAAL DATAARVAAA
LAARGVRHGD AVAVGLPRSW QLVCVLLGVL RLGARVVPLD AQSPPDRRDH VLTDSGAALL
VHTGEAAPDQ LPPGVGTVAS AALLTADEGE GSDVDGRTGA PLPPVTAPEV SFLFYTSGTT
GRPKGVAVRD AGVLRLARPG YVRLEPGARY ACLANPAFDA LSFEVWVPLL TGGCCVVVPD
ADVQSPERLA ETLLRERVDT AFVTTALFDA VVRAVPACFA GLGQLLVGGE QLNSRVVRAW
YRHNADSRTQ LHNVYGPTEC TTFALCHPVP RDFDAPVVPI GRPLPETGTA LVVPGTTRTA
APGEVAELLL SGTGVAAGYV DLPEETARRF VHLAGPDGRP VLHYRTGDLV RRDAQGDVTY
VGRVDRQVKV RGFRVEPGEL EQRIRTHPAV RQAYVCTRRA GGGGSDDGGE GPNELLAFVV
VDPGLTWEEF DGHLGAVLPA YMRPHRLHRL EALPLTANGK VDQAALLART DPPWRPDDDG
RRHGATADGD GAVLAEVLEL AARVLELPDP RPGDTWVACG GDSLKALRLR FEIRRRWGRD
LPQSAVLDGD LAALAAAVEA AGDDTGPAYP AVTAAGARSA PATGEQQRLW LIQQRSPHSR
AYDVRLAFAL DGAVDRTALR TGLRLLCARH PALRTGFEAS ADGLLQVVGE AYDPWVEPDG
AAEAGSGAAE DAFFAEPFDL ARPRMLRATL LPTAAGGTLL LHLHHVAVDG WSLNVLLHDL
SRAYADALSA GHPGNAAGPE AEQAAAPTPL DFAVWQEAWR SGAAYAAQRD KLLAHHARLA
DTTETPALRA AHPAAEPGAG LLHTELTGHG RDALDRLCAE LGLTRFPLLL AVYAWALYGV
TGRTRLRVAA PVAQRPVREF EDSVGMFANT VLLPLAVSPL GALREQLLLL ARDARTVLER
QDVALADVLH GRPGKAGGGP PFDFLFVLEN TDFGALTLPG CVTSPRWPVP AEAKCPLTLS
VVERPDGLAL LWEYAREHFT EAEAAAADAL FRRGLAALTG DPTADATPAE VVAGHRHALP
TPGRGAVGAP GWSTVAEGFA RQVARTPAAP ALMTAEGPVD YGTLDGMAEA LAAELLATYD
VPGGEQPCHV ALFMEPSAAH VVALLALARL NLTAVPLDPS YPPALLRQIL DRTAPLCVLL
PPDDATANGP ANGGGSAFDA VDPGGVPRLT VTLSPGTSGP ARAPVPHDGA RPLYTLFTSG
STGTPKGVRV YDRTLCNLLR WQESSDGPGG AAATQQFSML SFDVSFQEVF GTLCVGGCLH
LVRPGWRQDV PALLERLESA GIERLYLPFV ALQMLAEHGA HLGRHPSRLR EVVTAGEQLV
CTPAVRRWFA GMPGARLFNH YGPTETHVVS GLRLDGDPAL WPDRPAIGTP VDGAVLHVVD
EAGLPVPAGC PGELLIGGVI DTPCYLEEPG AGGPESADDD GLNVRRFTRL PYAEGLFYRS
GDRAAFDTDG LLHFLGRADD QLKVSGHRLE PGQVEAALLR HPAVVGAVVA VDGRELVACL
RCRDDAAPTP ADLRRHLAGL LPAHVRVDRF RLLAELPRTP SGKLDREAAL RAPAREPYAD
GTPDRTTHGA GGREQALSVR ESALVAAFEE ATGSPVGPDE TYFEAGASSL DLMRFHLRLT
AGLGLRLTVA DLFEHVTPRQ LARLVDGQGP DGAGDAEGTA GDTGTETGTR TAHGAGPADE
ATAVVGMAVR APGAPDLAAF WDLVTTGRSG IEHFDASPGL VGARSQLDGM LAFDPGRFGI
SPQEARLMDP QQRHLLMTCV EALAHAGVGD TGAVRVGLVA GAGENTYFQS MLREGDPAAL
PDGFQLALHH DKDFLATKAA YHLGLTGPAL TTQTACSSSL VAVHLAADLL RRGDADVMLA
GGVLVDPTLS DGYRYRPQHI FSPDGRCRPF SDDAAGTVGG SGAAVLVLKP LSRARRDGDT
VYAVLTGSAV NNDGAAKLSY SAPSVAGQRA AIRTALRRSG RTGADVAYVE AHGTGTRLGD
PVEADALRQA LGTTAPESCA LSSVKSQIGH LGAAAGAVGL VRAVLAVHHG VVPPTPGFRA
FNPEIGPDPA PFHVPTEAAP WPPERERVAA VSSFGIGGTN AHVVLEAGTT ADAVPTTAVA
PAHAAAGAGA GTGGVRVAGA VPLLVLSAAG EPQLRADAAR IADYLERRPD AYGQVLRHLQ
AGRAHGRLRR GAVCPDARAA VAWLRTENTT RAEADTSAPP VPAEGRTAAD LAGVWLAGRA
VAWPEGPAQA PWDFPPPAFD LTDHDFARAA ARSAGAVRDA GSVRSAGAPD TGVAVPERRP
EAEWLHQPQW VRLRRATTAA GAGTGVGPTR AVVLVTEGPA DPALADAFAA TGGRVVRVEG
AEGAEFARTG TDRFRADPVD PAQLRLVLDA FAGDTPGNDD SDGEGTAAPD RVDWVHALPL
ALDGPVSAAV LDRASRACLD TPAALVRAVS GTPYAALLRP WWLSYGARPV LGGVTRPEGA
LLAGVTEVAP QEGAPYGHWV DVAVPGPDGW ARQLAALLAG AEREALPRQL ALRGGHWWEQ
AVLPVTDPGP AAGTGAVWPA DARGDHVVLG GTGGLGTALA EWLLTHTAGR VLLLSRRPEP
PEALAPWADR VDLVAGDLAD EPLDALAARI AARVAARPYG LASVVHAAGT GAGGLTARRD
AAAMRRALAP KLRGALLAER LIAEHAPSLA VYCSSMSAHL GGVGQFDYAA GNALLDAFAH
HDPAYDAPPS TPYATGCSAP YGDGTARLTL AWDVWRETGM AVRALGGDAR HQAHLSVGLT
VAEGQRVFGR AVGLGLPHLL VSATDVAASR VFYAGAAPAP TGPARPEPEP RTEPGAERGA
EAGAERPAPE RSAWELVTAE LCGWLGLDGL DPDASLYDMG ADSLLLLSLI DTVEQHLGVE
LDLASLSHRV SLNEILDRLA DAGTPVPPPP GAAPVPVEVW QEGTGDDVLC LVHPVGGDVQ
AYRALVSALD PRLTVALIAD PALRDPDHPR WSIDERARHY LAALHARFPG TGWRHHLAGW
SFGAWVAAGM AAEAETAAAA AAAAAAGNGN GTGSGAGAYG GRVRSLHLLD PPSPGSGAVY
REYDETQLKT LFAAELGSGD GSGAGDGTDG NGTGARGRAY ADRLARCCLD NLRSMDGHRL
PRITTTPTRL WLAREPVEGL PPLGPPRERR ARWHAHLPDG AGTEVLGTTH YGLVRPPYAA
TVAADIEAAV ARSRPTPAAP GPETAAHPRP
//
