ID   A0A1L7F964_9PSEU        Unreviewed;      1293 AA.
AC   A0A1L7F964;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Amino acid adenylation enzyme/thioester reductase family protein {ECO:0000313|EMBL:APU21348.1};
GN   ORFNames=UA75_16700 {ECO:0000313|EMBL:APU21348.1};
OS   Actinoalloteichus sp. GBA129-24.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU21348.1, ECO:0000313|Proteomes:UP000185506};
RN   [1] {ECO:0000313|EMBL:APU21348.1, ECO:0000313|Proteomes:UP000185506}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GBA129-24 {ECO:0000313|EMBL:APU21348.1,
RC   ECO:0000313|Proteomes:UP000185506};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT   (=GBA129-24).";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; CP016077; APU21348.1; -; Genomic_DNA.
DR   RefSeq; WP_075741037.1; NZ_CP016077.1.
DR   STRING; 1612551.UA75_16700; -.
DR   KEGG; acti:UA75_16700; -.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000185506; Chromosome.
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: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; cd05930; A_NRPS; 1.
DR   CDD; cd19540; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
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; 3.30.559.30; 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; 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}.
FT   DOMAIN          974..1049
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          947..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1293 AA;  141532 MW;  531ECFD67A20BB51 CRC64;
     MIPLSYAQRR MWLTHQLEDR AETYNISPTF RLTGPLDHTA LVTAINDLID RHEILRTTYV
     TDAEDEPHQL VLPAEEALVR LPVVDVVPEE LSGPVNEVIA HHFDLSTEIP LRAHLFRCAE
     EEHVLVLVIH HIASDGVSGA PLARDLAVAY TARLEGRAPA WEPLAVQYKD YALWQRELLG
     DVTDPDSMAA KQAEYWRAEL EGVPQPLNLP LDRPRPERRS LQGDTVGVVV DPHVAAGLRR
     LAAEHGVTMA MVMQAGLGLL LGKLGGGDDV TIGSPIAGRT DEALADLVGF FVNTQVLRVD
     LSGDPSFAEL LARVREKALA AYEHQDLPLE MLVELINPDR SAAYQPLFQV MFAWQNWAKG
     EYALPGLEVG FEQHLVSTIM SDLFLSMTMD ESGALWGDLM YSTQLFDRET AEAITARLLR
     VLEQVAADAR TPVSAIDVLS ADEREWLLRG VNDTVAPVSV GTLPGAFEAQ VERDPDRLAV
     IGEQETLSYS EFNRRANRLA HWLVEQGAGP EQVVAVRIPR SVELMVAIFA VVKAGASYVP
     VDTELPPDRV RQLLESAQPL LVLDSTLPDV SGYPETNPRR ELSPDNAAYL IYTSGSTGGP
     KGVQVSHRSI MNRIEWGLAH FDVTPQDRIL LITSTSFDMS VPEMFAPLRM GAAVVVARPD
     GRKDPVYLAE LIQRERVTVA DFVPSLLEAF VAEPSAGKCT SLRWIEVAGE AFPAALANTF
     VDLLPGCAAH NLYGPTEATV EVLAYEHVPG ADRVPIGTPI WNTQVYVLDG ALRPVAPGVT
     GELYLAGTGL ARGYLGQTAL TSHRFVASPY GEPGARMYRT GDVVRWNKDG QLEYIGRTDF
     QVKLRGFRIE LGEIENVLAG HPGVARAAVI AREDGRGDKR LVAYVVPDPD AEATDGPDWI
     GRLPAELPAY LRERLPDYMV PSAVVPLAEL PLTPAGKLDR QALPAHDATI PTNGAPRTEP
     DGQAPVNAAT QSGGPRNAQE EKLCSLFGEL LGVEKVGIGD DFFTLGGHSL LATRLSARIR
     KHFGFDLPVR TIVRYPTVAE LSALMLTGGG ILTEDVDQYG VVLPLHDDPG TGKTPVWFLH
     GGGGLGWVFF SFAPYMRDRP AYALQARGCN GTDPLAASVR EMVDDYLDRI LEIQPEGPYN
     LVGWSFSGPV AHALAEALDR RGHEVGLLAI LDAMPSSGFK NLDGIEPTAF RKEVAEFMSE
     YINTGNIDDL LNMMGKVGAN NRAIMKEFDS PVYRGDMLYF HATQGKDWGS YAVHWRQHVL
     GSIEEYDVDA SHEYMHMPKP ADQIMRVIAG RLD
//