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Database: UniProt
Entry: A0A1P8F4V3_9CHLR
LinkDB: A0A1P8F4V3_9CHLR
Original site: A0A1P8F4V3_9CHLR 
ID   A0A1P8F4V3_9CHLR        Unreviewed;       487 AA.
AC   A0A1P8F4V3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:APV43517.1};
GN   ORFNames=Dform_00154 {ECO:0000313|EMBL:APV43517.1};
OS   Dehalogenimonas formicexedens.
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX   NCBI_TaxID=1839801 {ECO:0000313|EMBL:APV43517.1, ECO:0000313|Proteomes:UP000185934};
RN   [1] {ECO:0000313|Proteomes:UP000185934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSZ-14 {ECO:0000313|Proteomes:UP000185934};
RA   Key T.A., Bowman K.S., Lee I., Chun J., Albuquerque L., da Costa M.S.,
RA   Rainey F.A., Moe W.M.;
RT   "Dehalogenimonas formicexedens sp. nov., a chlorinated alkane respiring
RT   bacterium isolated from contaminated groundwater.";
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001818, ECO:0000256|HAMAP-
CC         Rule:MF_00022};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00022};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-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}.
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DR   EMBL; CP018258; APV43517.1; -; Genomic_DNA.
DR   RefSeq; WP_076003324.1; NZ_CP018258.1.
DR   AlphaFoldDB; A0A1P8F4V3; -.
DR   STRING; 1839801.Dform_00154; -.
DR   KEGG; dfo:Dform_00154; -.
DR   OrthoDB; 9807503at2; -.
DR   Proteomes; UP000185934; 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:UniProtKB-UniRule.
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   Metal-binding {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:UP000185934};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00022}.
FT   DOMAIN          4..316
FT                   /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00749"
FT   DOMAIN          329..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           247..251
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
FT   BINDING         250
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   487 AA;  54925 MW;  7C371BE6220B146B CRC64;
     MTDKVRVRYA PSPTGYPHVG NIRTALFNWL FARNQGGSFI VRIEDTDQAR YVEGAVEAIL
     DGLRWLGMDW DEGPEKNGAF GPYFQSQRLD RYRAAAEKLI AGGHAYRCYC SSARLDQMRA
     AQEAAKIPTG YDRHCRDKCE PGPEGVTPVV RFKMPLEGRT YFNDLIRGEV AFENALLDDF
     VLLKSDGFPT YHLANIVDDH DMAITHVMRA EEWLSSTPKH VQLYKAMGYE PPVFAHLPMI
     LGPDRSKLSK RHGAVSIIDY KNQGYLPETM VNFLALLGWS LDATTEIMDV KKVIENFSLD
     RISKTAAIFN IEKLDWMNGS YIRALSLDEF TDRARPFLEA GVPEAAAYDR DYVKSALALI
     QERVKKLGEL RDQPELTRFF FYQNLEYHAA DLVGKGMNTA LTRQALQATL DRLEKLEGFG
     IEAMENDLRP LAAELGLKPG QLFGCIRVAV TGQSVSPPLF QTMAVLGKDR ALARIREAIR
     KTRELAE
//
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