ID H4GKA9_9LACO Unreviewed; 499 AA.
AC H4GKA9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=PS3_8637 {ECO:0000313|EMBL:EHS85561.1};
OS Limosilactobacillus gastricus PS3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS85561.1, ECO:0000313|Proteomes:UP000004567};
RN [1] {ECO:0000313|EMBL:EHS85561.1, ECO:0000313|Proteomes:UP000004567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS3 {ECO:0000313|EMBL:EHS85561.1,
RC ECO:0000313|Proteomes:UP000004567};
RX PubMed=23846278;
RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M.,
RA Fernandez L.;
RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated from
RT Human Milk.";
RL Genome Announc. 1:E00489-E00413(2013).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001818, 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:EHS85561.1}.
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DR EMBL; AICN01000062; EHS85561.1; -; Genomic_DNA.
DR RefSeq; WP_007122492.1; NZ_AICN01000062.1.
DR AlphaFoldDB; H4GKA9; -.
DR STRING; 1144300.PS3_8637; -.
DR PATRIC; fig|1144300.3.peg.1377; -.
DR OrthoDB; 9807503at2; -.
DR Proteomes; UP000004567; 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; 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; IPR001412; aa-tRNA-synth_I_CS.
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; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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:UP000004567}.
FT DOMAIN 5..330
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 361..489
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT MOTIF 259..263
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ SEQUENCE 499 AA; 57694 MW; 9B65F37247665450 CRC64;
MAKNKVRVRY APSPTGHLHI GNARTALFNY LFARHYKGQF IIRIEDTDTK RNIEDGERSQ
LDNLKWMGLD WDEGPDKGGD FGPYRQSERR DLYDQYIQQL LDQDLAYKSY MTEDELEAVR
ERQKANHEMP HYEYEYAGMS ADEIASAQAA AEAKGLKPVI RFRVPNDAVY EWDDLVKGHL
SFESSSVGGD FVIQKRDGMP TYNFAVVVDD HLMQITHVFR GDDHVSNTPK QMMIYEALGW
DVPKFGHMSL IINTETGKKL SKRDESILQF IEQYRDLGYL PEALVNFIVL LGWSPEGEDE
IFSLKEFVKM YDEKRLSKSP AAFDRKKLRW INNQYMKLSS ADEVFNAAMP QLIEAGLMEK
HADPYQMEWM RRLVELFKRE ISYAHEIIDY VKPFVHGPAD IDDDAKEEMK AETAVVVLKA
FRDKIAAMDF MDATSVLAAI KAVQKETKIK GRQLWMPIRI AVTHESHGPE LPESIELFGQ
KTTLEHLDTM IDRIENNQL
//