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
//