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Database: UniProt
Entry: A0A2D0LFK8_9GAMM
LinkDB: A0A2D0LFK8_9GAMM
Original site: A0A2D0LFK8_9GAMM 
ID   A0A2D0LFK8_9GAMM        Unreviewed;      1075 AA.
AC   A0A2D0LFK8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Amino acid adenylation enzyme/thioester reductase family protein,thioester reductase-like protein {ECO:0000313|EMBL:PHM74478.1};
GN   ORFNames=Xkoz_00716 {ECO:0000313|EMBL:PHM74478.1};
OS   Xenorhabdus kozodoii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351676 {ECO:0000313|EMBL:PHM74478.1, ECO:0000313|Proteomes:UP000221101};
RN   [1] {ECO:0000313|EMBL:PHM74478.1, ECO:0000313|Proteomes:UP000221101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17907 {ECO:0000313|EMBL:PHM74478.1,
RC   ECO:0000313|Proteomes:UP000221101};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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:PHM74478.1}.
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DR   EMBL; NJCX01000004; PHM74478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0LFK8; -.
DR   Proteomes; UP000221101; Unassembled WGS sequence.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05235; SDR_e1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 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   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
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; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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          566..641
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1075 AA;  119071 MW;  5906130E7A5576C5 CRC64;
     MPLFIMKIDE TNEALNESII MNTYTHKAIL HTALTTGQKN APAVAPEFTS IISCMTAELV
     PWFKSVPSRL SELAKSIPNE IAVSDPYETL TFGELDQRIE KAAYILRYHG AKMGSSVAIA
     AQRGIAWFIT MQATWRIGAV YIPLNTLMPE KRLNDILASL PESILVSDDT VSAGLKASTF
     IPMNAILNPM ANAETAENMD IPVLGDHPAY VMFTSGSTGL PKAVQVQHDN LTACLCGFGK
     LLSISPRDHM LALTTFSFDI SVLELLLTVV HGGSIYIASI DTQRDAMALS ETLSDPQFTF
     AQATPVTWSM ALNAGWKPRP AMSMLCGGEA LSQDLADKLT ATGSTLWNVY GPTETTIWST
     AYCMKKGDKV QLGGPIPGTS IMVVDEHLRP VPKGTVGEIL IGGLGVTAGY RNNPTETAKR
     YVPDMTQKGK RAYLTGDMAR MLEDGSLIYM GRQDDQVKVR GHRIELGEIE IALRKQYGVQ
     DAIIRVAGSG DFAKIQAFVL FNPTLVVPEE WVRETQRSLR EILHDAWIPT EYYRIPYIPL
     TNSGKRDKKR LEEVAERLNA SHDRVPPRTE TEKRVDEIWR GLLGTDIFGI TDDFFQIGGH
     SILVARMVEH IDNAFSLRVP ISAIYVEPTI AKIAAILDEI MAARQTNPTQ LAGTYHNEAL
     IRQHAKRLKD DVYLKEGVRP DGLAHANGYQ PDKILLTGAT GYLGLHLLEQ LLKQTSARVI
     CLCRASDAEH ARARLKAGCN NYHIDIGDGL ERVDIILGDL GQPRFGLLPE SWAQLAEEID
     VIYHNGAWVN FIYPYSALKS INVDGTRTAL ELACTARLKH FHYVSSVNAL YATQSPRPYL
     EDDRAMGEPV RDPSGYSGSK WVSEGIINIA RQRGVPVSIY RPGLILGHTR TGAAQGNDYL
     IASLKGYLAM GFYPDHALLL DIVPVDYVAS ALVHISRQPE SNGKFFNLFN PEQVSIRQFF
     DWVQDFGYIL NPVPFNEGKE KILALDDTHP LYPLIPLIRD MTERPYRALD PAYVNEIHPE
     RELKNTLAGL AGSPIRCPTI TAEYVHQVLR YLIGTGFLPA ALSERFKKEA ISWND
//
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