ID A0A1M6FMX4_9FIRM Unreviewed; 486 AA.
AC A0A1M6FMX4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02745691_01152 {ECO:0000313|EMBL:SHI99061.1};
OS Parasporobacterium paucivorans DSM 15970.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Parasporobacterium.
OX NCBI_TaxID=1122934 {ECO:0000313|EMBL:SHI99061.1, ECO:0000313|Proteomes:UP000184342};
RN [1] {ECO:0000313|EMBL:SHI99061.1, ECO:0000313|Proteomes:UP000184342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15970 {ECO:0000313|EMBL:SHI99061.1,
RC ECO:0000313|Proteomes:UP000184342};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQYT01000010; SHI99061.1; -; Genomic_DNA.
DR RefSeq; WP_073993410.1; NZ_FQYT01000010.1.
DR AlphaFoldDB; A0A1M6FMX4; -.
DR STRING; 1122934.SAMN02745691_01152; -.
DR OrthoDB; 9807503at2; -.
DR Proteomes; UP000184342; 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:UP000184342}.
FT DOMAIN 4..322
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 335..479
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 11..21
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT MOTIF 253..257
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ SEQUENCE 486 AA; 55585 MW; B400B220438DAF03 CRC64;
MDKKIRTRFA PSPTGKMHVG NLRTALYEYL IAKHEGGDFI LRIEDTDQER YVEGALEIIY
NTLSLAGLEH DEGPDKDGGS GPYVQSERQA TGMYMEYAKM LVEKGEAYYC FCDRERLDSL
KQVIEGKEIS IYDKHCLGLT KEEAASNLDK GIPFVIRQNN PREGQTTFVD EIYGEISVDN
SELDDMVLMK SDGYPTYNFA NVVDDHLMKI THVVRGNEYL SSSPKYNRLY AAFGWEVPVY
IHLPLITDSD HKKLSKRSGH SSFEDLIEQG FLSEAIVNYV AMLGWSPEDN REIFSLEELA
RDFNYHNISK SPAVFDIVKL KWMNGEYIKA MDNKRFYEMA EPVLKEAIHK DLDSGKILDL
VKTRIEVLPD IREMVDFLDD LPDYDIEMYT HKKMKTNPEI ALAILEELLP VLEKHEDYTV
SSLHDLIMDF ISVKGVKNGI VLWPLRTAVS GKQSTPGGAY EIMEILGKEE SLQRVRIGIE
KLSQEK
//
