ID A0A1E8FUP3_9MICC Unreviewed; 508 AA.
AC A0A1E8FUP3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-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=BIU82_01055 {ECO:0000313|EMBL:OFI39679.1};
OS Arthrobacter sp. SW1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1920889 {ECO:0000313|EMBL:OFI39679.1, ECO:0000313|Proteomes:UP000176251};
RN [1] {ECO:0000313|EMBL:OFI39679.1, ECO:0000313|Proteomes:UP000176251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW1 {ECO:0000313|EMBL:OFI39679.1,
RC ECO:0000313|Proteomes:UP000176251};
RA Shaligram S.M., Kumbhare S.V., Pawar S., Dhotre D., Muddeshwar M.G.,
RA Kapley A.;
RT "Genomic insights of Arthrobacter sp. strain SW1 for secondary metabolite
RT production.";
RL Submitted (SEP-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:OFI39679.1}.
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DR EMBL; MJLT01000001; OFI39679.1; -; Genomic_DNA.
DR RefSeq; WP_070347598.1; NZ_MJLT01000001.1.
DR AlphaFoldDB; A0A1E8FUP3; -.
DR SMR; A0A1E8FUP3; -.
DR STRING; 1920889.BIU82_01055; -.
DR OrthoDB; 9807503at2; -.
DR Proteomes; UP000176251; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 1.10.8.70; Glutamate-tRNA synthetase, class I, anticodon-binding domain 1; 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; IPR020752; Glu-tRNA-synth_I_codon-bd_sub1.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
DR InterPro; IPR033910; GluRS_core.
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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000176251}.
FT DOMAIN 25..341
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 358..505
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 31..41
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT MOTIF 275..279
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ SEQUENCE 508 AA; 56265 MW; 63D38193CF588A9D CRC64;
MTTAPASNSA ANSAAIPAVT AETPVRVRFC PSPTGTPHVG LIRTALFNWA YARHTKGTLV
FRIEDTDAAR DSEESYHQLL DALKWLGITW DEGVEVGGPH EPYRQSQRSD IYQDVIAKLK
AGGHIYESYS TPEEIEARHR AAGRDPKLGY DGFDRHITEE QLAQYKAEGR EPVLRLHMPD
EDITFTDLVR GEITFKAGSV PDFAVVRANG APLYTLVNPV DDALMGITHV LRGEDLLSST
PRQIALYRAL HAIGVAEYMP EFGHLPYVMG QGNKKLSKRD PESSLFLHRE RGFIREGLLN
YLSLLGWSLS ADEDIFTVEQ LVENFDIHDV LGNPARFDLK KAEAINGTHV RMLSPEDFRE
RLVPYLRDAG LVGEILTDRQ EEILTEAAPL VQERITLLGE APEMLAFLFK ADDAIDVADD
ARKGLPENLG EVLDAALAAL EPIADWTAEN IQTALKQALV EDLGIKPRLA FGPVRTGISG
RRVSPPLFES MVILGKESSL ARLRTFRG
//
