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Database: UniProt
Entry: A0A1G8BHJ8_9PSEU
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ID   A0A1G8BHJ8_9PSEU        Unreviewed;      1536 AA.
AC   A0A1G8BHJ8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Amino acid adenylation domain-containing protein/thioester reductase domain-containing protein {ECO:0000313|EMBL:SDH32715.1};
GN   ORFNames=SAMN05216553_11974 {ECO:0000313|EMBL:SDH32715.1};
OS   Lentzea fradiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=200378 {ECO:0000313|EMBL:SDH32715.1, ECO:0000313|Proteomes:UP000199623};
RN   [1] {ECO:0000313|Proteomes:UP000199623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3506 {ECO:0000313|Proteomes:UP000199623};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNCC01000019; SDH32715.1; -; Genomic_DNA.
DR   STRING; 200378.SAMN05216553_11974; -.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000199623; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 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; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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}.
FT   DOMAIN          1057..1132
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          81..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1536 AA;  166286 MW;  6D6C3E57F6669560 CRC64;
     MNSPLESAVL ELARTVTGVA DLSAADSLSR RCGGPDALPR VCAAVRAVFA AGLTGELVRG
     ADTVGELARA VERLREGAPR RPSLSAGLAQ RRGDSVPASS GQSGIWLADQ YAPSSTAYNG
     PFHVLFPEAL DPEALREAVR RVVDRHEVLR TNLLLRDGVL TQVVSPEARF RYEVREFSSD
     DEPAAIASEV ARTRVDLGAD PVVTVVCATR AGGPRETAVV CNIHHAASDA ASAGLFLTEL
     MARYDEVVTG LPTADRGDRP QYADFARWHE LRLAGPELPR LLDHWTDRLG GELPALDLPT
     DRPRPATRRF AGDVLPFTVP APLVRELHAL GAAEGVTLFM IAHAAYALLL SRYARQDEVA
     VGTPVSLRDP AEAEDVIGYL VNMVVLRHRL DDTATVRDLL RAVRDEAADA MRHKWAPFEK
     VIERVRPKRG GGYSPLIQTM LVLTPPGSTC FERGGRRLPI HRDVGHGAKY DLSLVLQPGD
     AGELAASFEY DTDLFDAGTV RGLGERLVHV LAEFARRPDA ALGEVRLLSP REERALLARD
     DRVAERTPPR PTSELFEERV AKAPDAVAVE HEDRSLTYRE LNEQANRLAH LLRERGTGVG
     DRVGLYLRRS VESVVALLGV LKSGAAYVPV DPSYPRDRVE DMLADAGVRL IITDSASASG
     LPATAQRLEL DREDLSGLPA DDPGRVKRPE DEVYVVHTSG STGRPKGVVI RDETVANLVE
     VQDRVSPVGA TGRTLQYMSL SFDVSVMEIL GTLCAGGTLV LISEEVRKDL HALAEFLRRH
     DIARVYLPYV AVQGLAAIAA DAGLRLEALR EVASVGEQLV VSPQIRRFFA EHPDARLLNM
     YGPSETHLAT WHEVGGDPAS WPEAPAIGHG IAGLRLAVLD RRGAVVPPGV PGELHLGGPV
     LSPGYHRRPE ETEQRFLPDP FHPGEVLYRT GDLVRRTRDG LEYLGRVDDQ IKIRGYRIEP
     AEVEAAIDAL DLVAASAVTA VDVAPGDRRL VAFVAGGPED PREVARALTG VLPDHMVPAH
     VVRLERLPLT PSGKADRKAL RGMFSLEDTR SDAPAEPPAT PLEESVARQW AELLGGGAVG
     RHDDFFTLGG HSIMATELVY RLRREHDVDL PLRVMLENPT VAGMAARIAE IRDTGTTAAP
     RGLDLPAEVR LPEGFAVSGT PVADDEVTDV LLTGATGFLG AFLVRDLLRT TNLRVHCLVR
     AGDAERAWAR LLDTARRYGI EEALDPARVV AVPGDLTRER LGLSEEDHDA LAEAVGVVYH
     AAAHINFMLP YSSVKATNVD GTSRVVAFAA HRRVKRLHHM STIAVFSPAE PEGVLTEEST
     PLAPEALGIG YTQSKWVAER IVSQAGNAGL PVTIYRIGRV SGDSATGACQ PDDFLWRQVK
     SFIQLGAAPP GDTLTTDLLP VDYVARAVVA LSRDPGAHDR TLHLFHPRGS DFDTVYQGIR
     ACGHDVRVVA EDHWWELLER SAAAPGGNAL AATVPLFREG ALELGDNTYR NDLTATLLER
     LGLPFPDIEP GAVARMIRYF EGVGELAEAE VPEPVA
//
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