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Database: UniProt
Entry: A0A197SM85_9ACTN
LinkDB: A0A197SM85_9ACTN
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ID   A0A197SM85_9ACTN        Unreviewed;       454 AA.
AC   A0A197SM85;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            Short=GluRS {ECO:0000256|HAMAP-Rule:MF_00022};
GN   Name=gltX {ECO:0000256|HAMAP-Rule:MF_00022};
GN   ORFNames=A8W25_15990 {ECO:0000313|EMBL:OAR23971.1};
OS   Streptomyces sp. ERV7.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1322334 {ECO:0000313|EMBL:OAR23971.1, ECO:0000313|Proteomes:UP000078470};
RN   [1] {ECO:0000313|EMBL:OAR23971.1, ECO:0000313|Proteomes:UP000078470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERV7 {ECO:0000313|EMBL:OAR23971.1,
RC   ECO:0000313|Proteomes:UP000078470};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC       step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC       then transferred to the acceptor end of tRNA(Glu). {ECO:0000256|HAMAP-
CC       Rule:MF_00022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00022};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007894, ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00022}.
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:OAR23971.1}.
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DR   EMBL; LYOY01000040; OAR23971.1; -; Genomic_DNA.
DR   RefSeq; WP_067162442.1; NZ_LYOY01000040.1.
DR   AlphaFoldDB; A0A197SM85; -.
DR   STRING; 1322334.A8W25_15990; -.
DR   Proteomes; UP000078470; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00022};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00022}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00022};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00022};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00022}; Reference proteome {ECO:0000313|Proteomes:UP000078470}.
FT   DOMAIN          2..289
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          304..449
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
FT   MOTIF           221..225
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   454 AA;  50218 MW;  3BB395A0B035B058 CRC64;
     MFHVGGARSA LYNWAVARQS GGTFVLRIED TDAARNKPEW TGGIIGALAS IGISRDDPAF
     EGPYFQSQNA DRHREAAQRL YAAGRAYYCD CTREQVQRRT GSQQLGYDGF CRGRALEHAE
     GRALRFRTPD EGATVVVDLV RGEPAFPNSA IEDFVIARGD GSPVFLIANV VDDMSEGITQ
     VIRGEEHLSN TPKQQLLWEA LGAAPPVWAH LPVIVNDKRQ KLSKRRDKVA LEDYLAEGYL
     PKAMVNYLML LGWGPGGDME IRPQEELERL FRVKDVNGSS AFFDVKKLSA FNGAYVRDLE
     VDEFIDACAP WLTEPYATWA PESFDATAFA TVAPLAQTRL TVLSEITKYV DWLFLDEPVY
     DEASWTKAMK PGADAILQDT RERYATTPWD AEALKAALEE VAAAHDLKLG KAQAPVRVAV
     TGRTVGLPLF ESLEVLGREH TLNRLDAALR KLAG
//
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