ID   A0A2U2Z9I4_9ACTN        Unreviewed;      1300 AA.
AC   A0A2U2Z9I4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Amino acid adenylation protein {ECO:0000313|EMBL:PWI08957.1};
GN   ORFNames=DIZ27_19920 {ECO:0000313|EMBL:PWI08957.1};
OS   Streptomyces sp. NWU339.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI08957.1, ECO:0000313|Proteomes:UP000245372};
RN   [1] {ECO:0000313|EMBL:PWI08957.1, ECO:0000313|Proteomes:UP000245372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NWU339 {ECO:0000313|EMBL:PWI08957.1,
RC   ECO:0000313|Proteomes:UP000245372};
RA   Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT   "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT   South African rhizosphere soils.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI08957.1}.
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DR   EMBL; QFRK01000015; PWI08957.1; -; Genomic_DNA.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000245372; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd02142; McbC_SagB-like_oxidoreductase; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.109.10; NADH Oxidase; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020459; AMP-binding.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR000415; Nitroreductase-like.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
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; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245372}.
FT   DOMAIN          949..1024
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1027..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1300 AA;  142106 MW;  AC347AE641B24698 CRC64;
     MSTVNNTGKT GIESAGTEES AGVGDLIELL DAQVRTRPDA VAVGHGNDTL TFRELTEAAR
     YLALHLRTLG VGKDTCVGLF TSPGLQQAVG VWGILRSGGA YLPLSPEYPD ERIRTMIEDS
     GITVVHTEEK LLDRARELAG TGVRIVTERN VEEFRKSLDE NMQSIPLPQP GPEDLAYVIY
     TSGSTGRPKG VMIEHRAIAH QMTWLKSAYG LGPDKVVLQK TPLSFDAAQW EFLAPACGAR
     TVMAPAGSHR DPGRIIDEIA VHSVTTLQCV PTLLAALLDH QDMSRCTSLQ QIFSGGESLS
     RKLALHCTRT LPHCTLVNLY GPTECTINTS AHTVDPAVLA PEDGPRSVPI GRPVPGLRYH
     VLDDRGRPAG PGETGELHIS GVQLARGYLH RPDLTAEHFV PSPHPAPHDR LYRTGDLAHW
     NADGTVQFTG RADNQVKLRG HRIELDEIRL AIEAHDWVKN AAVLVRDDPR TGFQNLVACL
     ELSPREAALM DQGTFGDHHI SKDSRLQVRA QLSTAGVRDD LAEARAVDLP GAEATPEQRR
     RAFARKTYRF YEGGAPTEQD ILAALSRVVP SAPPRRPEQL TLTELGAILR DFGPHTSAER
     LLPKYAYASP GSLYATQLYA EITGCLPGLA PGLYYYHPLR HQLVLVRPAH ATDAAPGITF
     HFVGRRSAIE PVYKTNIQEV LEIETGHMLG LFDEILPVYG LGLRTLPHDP RVCDRCGCAD
     DDPCLGSYAL TSADPGTRPE WRDRVDVHVQ IHPGSGTGLR SGQYRHRAGR LERIADELVL
     RRHVIAINQQ VYQRASLGIT LTVHTPGDEP EYVNLGRALQ YLQHNTAGLG FMPAGYSSRS
     GRDLPAARRM TTLLEGLGLP TGPLYFCVGG RISDDQIAHE GMYEDTVHMK GPAELVKDDL
     AARLPEFMVP NQILILERLP HTANGKLDVQ DLTELADTAV ARGVRPVVPP RNRTEARLCE
     LWKAALHRDV ISVRDDFFAC GGNSLIAVSL VHRVNREFGC SLPLQVLFTA PTVEQLAERI
     AADTAPPPRL VPLSRDHRAA HPRPDGTSDR PVLCWPGLGG YAMNLRLLAS RLAEGPDSHT
     LYGIQAYGLN EGEIPHDSLE EMAAADVRAL RRVQPEGPYT LWGYSFGARV AFTAARRLEH
     SGEEVDRLVL LAPGSPRLPG PPSWTAAGAD FGDRTFRTIL YSVFAGRTDG PLLDACLREG
     TDEESFARFV LRHFPDLGPT TVRRVIRVAC RTYGWEPAPG PVTAPVTVLV AHGDEESFIE
     RDPAFAAGAS TVVRLDTTHY GLLRDPGVDE LAHVIRHSII
//