ID   SYE_NOSP7               Reviewed;         481 AA.
AC   B2IYI1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=Npun_R1357;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RX   PubMed=23463784; DOI=10.1104/pp.112.213116;
RA   Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT   "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT   Cyanobacterium-Plant Symbiosis.";
RL   Plant Physiol. 161:1984-1992(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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00022};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACC80068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001037; ACC80068.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041565245.1; NC_010628.1.
DR   AlphaFoldDB; B2IYI1; -.
DR   SMR; B2IYI1; -.
DR   STRING; 63737.Npun_R1357; -.
DR   EnsemblBacteria; ACC80068; ACC80068; Npun_R1357.
DR   KEGG; npu:Npun_R1357; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_0_3; -.
DR   OrthoDB; 9807503at2; -.
DR   PhylomeDB; B2IYI1; -.
DR   Proteomes; UP000001191; Chromosome.
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; 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; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000367721"
FT   MOTIF           9..19
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           247..251
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   481 AA;  54437 MW;  9AF27CA5C6F9CCC6 CRC64;
     MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA RHHGGKFILR IEDTDLERSR PEYTDNILEG
     LRWLGLNWDE GPFFQSQRLD LYKEAVQKLL DQGLAYRCYT TSEELEALRE AQKARGEAPR
     YDNRHRNLTP EQRAAYEAEG RSYVIRFKIE DGREIVWNDL VRGKMSWRGS DLGGDMVIAR
     ASEEGSGQPL YNFVVVVDDI DMQITHVIRG EDHIANTAKQ ILLYEAMGAK IPEFSHTPLI
     LNMEGRKLSK RDGVTSISEF QKMGFTAEGL VNYMTLLGWS PPDSTQEIFT LETAAKEFGF
     ERVNKAGAKF DWDKLDWLNS QYIHNTPVDK LTDLLIPFWE AAGYKFDGGR DRAWLEQLVT
     LISQSLTRLV DAVPQSQLFF SDTVEFSEEG STQLKQEGST AVLEAIVTAL ENQPQLSEAA
     AQDIIKQVVK EQKVKKGLVM RSLRAALTGD VHGPDLIQSW LLLNQIGLDK SRLSRAITEA
     N
//