ID A0A0P7KI00_9MOLU Unreviewed; 445 AA.
AC A0A0P7KI00;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 ECO:0000313|EMBL:QLL36729.1};
GN ORFNames=EPWB_v2c0940 {ECO:0000313|EMBL:QLL36729.1};
OS 'Echinacea purpurea' witches'-broom phytoplasma.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrII (Peanut WB group).
OX NCBI_TaxID=1123738 {ECO:0000313|EMBL:QLL36729.1, ECO:0000313|Proteomes:UP000050566};
RN [1] {ECO:0000313|EMBL:QLL36729.1, ECO:0000313|Proteomes:UP000050566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCHU2014 {ECO:0000313|EMBL:QLL36729.1,
RC ECO:0000313|Proteomes:UP000050566};
RX PubMed=26607900;
RA Chang S.H., Cho S.T., Chen C.L., Yang J.Y., Kuo C.H.;
RT "Draft Genome Sequence of a 16SrII-A Subgroup Phytoplasma Associated with
RT Purple Coneflower (Echinacea purpurea) Witches' Broom Disease in Taiwan.";
RL Genome Announc. 3:e01398-e01315(2015).
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; CP040925; QLL36729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7KI00; -.
DR Proteomes; UP000050566; 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; 3.40.50.620; HUPs; 2.
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; 2.
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:UP000050566}.
FT DOMAIN 4..112
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 113..286
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT DOMAIN 312..440
FT /note="Aminoacyl-tRNA synthetase class I anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19269"
FT MOTIF 216..220
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ SEQUENCE 445 AA; 52794 MW; BDB06BE22A574479 CRC64;
MESVRLRYAP SPTGNGLHIG NARTAFFNYL FAHLFKGSFI IRIEDTDTIR NITGSEEKQL
SQLKWLGLDW SEGPDIGGCY GPYRQSERLL IYEKYTRLLL EKQLAYKVYS DENKNDYVVR
FRVPKDQQYS FVDLIRGPIK FASKDIEDWI ILKENGYPTY NYAVAIDDHL MKISHIFRGE
EHITNTPKQI MIYQAFNWDI PCFAHMSLIL DKNKKKMSKR NFDAIQFIEQ YQNLGYLPEA
ILNFLFFLGF SPQTNQNILN KELMINLFNV KRFIKDPAVF DIDKLNFINK EYLKKLSLEE
LVIRVKFFFQ QFNIDLQDDQ LSKLVILLRD RLCYVKEIIE IYRWFFETEH KITDELKLFL
LKNKGYEVIP ILSELLNKLD IFQSLNLKQI ILNLKNHFNI ELKLLFKIVR ILCTCQLQGP
NLFDYLELLG KDKVLNNLEK FKLIS
//
