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Database: UniProt
Entry: J9A691_9PROT
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Original site: J9A691_9PROT 
ID   J9A691_9PROT            Unreviewed;       452 AA.
AC   J9A691;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=IMCC14465_03040 {ECO:0000313|EMBL:EJW21910.1};
OS   alpha proteobacterium IMCC14465.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX   NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW21910.1, ECO:0000313|Proteomes:UP000004836};
RN   [1] {ECO:0000313|EMBL:EJW21910.1, ECO:0000313|Proteomes:UP000004836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW21910.1,
RC   ECO:0000313|Proteomes:UP000004836};
RX   PubMed=23209213; DOI=10.1128/JB.01888-12;
RA   Yang S.J., Kang I., Cho J.C.;
RT   "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT   to the PS1 Clade of Alphaproteobacteria.";
RL   J. Bacteriol. 194:6952-6953(2012).
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:EJW21910.1}.
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DR   EMBL; ALYF01000002; EJW21910.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9A691; -.
DR   STRING; 1220535.IMCC14465_03040; -.
DR   PATRIC; fig|1220535.3.peg.301; -.
DR   eggNOG; COG0008; Bacteria.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000004836; 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; 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; 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:UP000004836}.
FT   DOMAIN          3..310
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          375..451
FT                   /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF19269"
FT   MOTIF           9..19
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   MOTIF           243..247
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   452 AA;  50256 MW;  25CC48275D1C255E CRC64;
     MSIITRFAPS PTGRLHVGNA RTALFCALYA KANGGQFMLR LDDTDAERST EAFAQGIIED
     LAWLGLPHDL TAKQSDRFDA YDEAFEKLKD MGLVYACYET PDELDLKRKR QRARGKPPVY
     DRAALELSDD EKAKLEAEGR TPHWRFKLSG NKVSWQDLVR GDQLVDTSSL SDPVLVRADG
     TYLYTLPSVV DDLDFNITHI IRGEDHVTNS AAQIELIMAL AGQDAIIPVF AHHPLLVMAD
     GSALSKRLGS LSLESLREDG IDPMSINSLI ARLGTPDPVE THSDMAALIA GFDLTRLGRA
     PARFDPAELQ RLNVKLLQHL PFERVADKLS HLGVTYEDEQ AGMLFWDTVK GNIDRLEDAV
     GLWQIIQGPV ESVIDAEDRD YLDMALACLP AEPWDETSWS SWTSELKQST GRKGKELFMP
     LRKAMTGQSH GPEMKNLLLL IGPTHVKNRL EG
//
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