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Database: UniProt
Entry: G2NLR8_STREK
LinkDB: G2NLR8_STREK
Original site: G2NLR8_STREK 
ID   G2NLR8_STREK            Unreviewed;       526 AA.
AC   G2NLR8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:AEN11666.1};
GN   ORFNames=SACTE_3821 {ECO:0000313|EMBL:AEN11666.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN11666.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN11666.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN11666.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
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DR   EMBL; CP002993; AEN11666.1; -; Genomic_DNA.
DR   RefSeq; WP_014047642.1; NC_015953.1.
DR   AlphaFoldDB; G2NLR8; -.
DR   STRING; 862751.SACTE_3821; -.
DR   KEGG; ssx:SACTE_3821; -.
DR   PATRIC; fig|862751.12.peg.3965; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_2_11; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05904; 4CL; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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   PANTHER; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:AEN11666.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397}.
FT   DOMAIN          25..386
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          438..513
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   526 AA;  56402 MW;  9ABFA6E53FF16EC8 CRC64;
     MVFRSEYADV PALDTPIHDA VLGQATERFG DTVALIDGTD GTSVTYAQLD TFHRRIAAHL
     AEAGLRKGDV LALHSPNTIA YPAVFYGATR AGAAVTTVHP LATAEEFAKQ LTDSTARWIV
     TVSLFLDTAR QAAELAGGVE RILVCDRAEG HTSVLDMLGS TAPEPRITFD PAEDVAALPY
     SSGTTGTPKG VMLTHRSIGT NLEQLRPFIP LEPGDTILAV LPFFHIYGLT ALMNVPLRCG
     ATVVVLPRFD LEQFLRAVQE HRISGLYVAP PIVLALAKHP AVGAYDLSSL RYVVSAAAPL
     DADLAAACSA RLGLPPVRQA YGMTELSPGT HVVPLDAENP PPGAVGKLLP GTEMRIVSLT
     DPGTDLGTGA DGEILIRGPQ VMKGYLGRPD ATAAMIDPDG WLHTGDVGRV DEDGWLYVVD
     RVKELIKYKG YQVAPADLEA LLLTHDAIAD AAVIGVRDDD GNEVPKAYVV RRQDTEDLTA
     DAVMAYVAER AAPYKKVRQV EFIDSVPRAV SGKILRRELR DREKQS
//
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