ID   A0A1I5AES9_9ACTN        Unreviewed;      1314 AA.
AC   A0A1I5AES9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SFN60943.1};
GN   ORFNames=SAMN04489713_102569 {ECO:0000313|EMBL:SFN60943.1};
OS   Actinomadura madurae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=1993 {ECO:0000313|EMBL:SFN60943.1, ECO:0000313|Proteomes:UP000183413};
RN   [1] {ECO:0000313|EMBL:SFN60943.1, ECO:0000313|Proteomes:UP000183413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43067 {ECO:0000313|EMBL:SFN60943.1,
RC   ECO:0000313|Proteomes:UP000183413};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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; FOVH01000002; SFN60943.1; -; Genomic_DNA.
DR   RefSeq; WP_075020445.1; NZ_FOVH01000002.1.
DR   STRING; 1993.SAMN04489713_102569; -.
DR   eggNOG; COG1020; Bacteria.
DR   InParanoid; A0A1I5AES9; -.
DR   Proteomes; UP000183413; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic 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:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0008610; P:lipid 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; cd12117; A_NRPS_Srf_like; 1.
DR   CDD; cd19543; DCL_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
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:UP000183413}.
FT   DOMAIN          976..1050
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          958..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1314 AA;  141694 MW;  3909A7E3D1A07BAC CRC64;
     MSTSQLEDIL PLSPLQQGLF FHALYDSGHD VYTAQIVFDL RGPLDGEALR AAAGTLLRRH
     ANLRAGFRQR KEGSPVQVVH RTVRLPWREE DLSALPEAER ETRARDLADA ERARPFDMAR
     PPLLRFLLLK LSDGLHRMVF TNHHILLDGW STPVLQTELF ALYLAKGDDT GMPRVAPYKN
     YLAWLARQDR AAAEDAWRRA LDGVHEPTLV APGAGDPVTG APGRVRTRLT EELTSALNAR
     ARAQGVTLNT VLQLAWGTLL GRLTGSTDVV FGAAVSGRPP ELPGVEQMIG LFINTLPIRV
     RVRPADTVAQ ALTRLQDEQA ALMQHHHLGL SDIQRLTGTG TLFDTMTVLE NYPFDPDAAG
     TDLGGLSLHD VAGYDASHYP LTFAAVPGRG LSLRVDHRTD FCGEAEAARL MRRLTRILDA
     IAYHPDLPLG RMDVLDEDER AKVLRDWQGP ATARRPGTLT ARFAAQAART PDAVAVRAAG
     RSLGYAELNA RANRLAHLLL GLGVGPETPV AVLLERSAET VVATLAILKA GGAYAPIHHG
     HPPERMAWAV AEVGAPVLLV DSVMRDRADG LGTSARIVVV DDDPRIAAQP GTDPGVECHP
     EQLACVFFTS GSTGTPKGVM ISHRDAVDLA TEERLGNGAH DRVLVHSPHA FDASTYEMWT
     PLLRGGTAVV APPGHLDGEA LEEIITAEDL TGLFITTTLF NLVADERPHA FAGLREVLTG
     GETGSPAAMR KVLAACPDTE VCNMYGPTEA TTYTTLAPQR APLADPSETT PALGRPFDDM
     RVYVLDPGLR PVPPGVVGEA YLAGAGVGRG YLRRPSLTAE RYVADPFGPP GGRMYRTGDL
     VRWRPDGRLD YVDRADSQVK VRGFRIELGE IEAAVAAHPA VANVAVIARE DTPGVKTLVA
     YVIAPDLAPE EDGPPQPPAA QPTVEGLREF VARKLPEYMV PAAFVRLDTF PVGPNGKLDR
     RALPAPDHGG AAAGRAPRTP AEERLCAIVA DVLGLGRVGA DVSFFDLGGD SIAALKLATR
     ARNAGIELTP RDVFTHQTVE ALARAGEPED RLGFEVLLPI RVSGTRPPIF FVHPAGGLAW
     SYLQLQRHLG PGQPAYGLQN RAFTRAEPPG SVEEMARDYV EEIRAVQPSG PYHLAGWSLG
     GLVAYEMAVQ LQSAGERVGL LAVIDAYHGQ DLESERREIL PELLESIGID ATMVAEDGNP
     DMAQIMAVLA ERDDALATLG EDDLVNVYRS YESGLRQAEE YRPGRFRGDV LFFTAMRGRS
     AAAPTGRSNW GPLVEGEIED YPLDADHHLL MEPGPAAEMG AVLAAKLDKL HSTH
//