SYE_HALMA
ID SYE_HALMA Reviewed; 579 AA.
AC Q5V5N9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02076};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_02076};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02076};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_02076};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_02076}; OrderedLocusNames=rrnAC0085;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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_02076}.
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_02076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02076}.
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DR EMBL; AY596297; AAV45163.1; -; Genomic_DNA.
DR RefSeq; WP_011222809.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V5N9; -.
DR SMR; Q5V5N9; -.
DR STRING; 272569.rrnAC0085; -.
DR EnsemblBacteria; AAV45163; AAV45163; rrnAC0085.
DR GeneID; 40154398; -.
DR KEGG; hma:rrnAC0085; -.
DR PATRIC; fig|272569.17.peg.891; -.
DR eggNOG; arCOG04302; Archaea.
DR HOGENOM; CLU_001882_1_3_2; -.
DR OMA; MRFAPNP; -.
DR Proteomes; UP000001169; Chromosome I.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.240.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR007527; Znf_SWIM.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..579
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119714"
FT MOTIF 114..124
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ SEQUENCE 579 AA; 65006 MW; 2B4FF0D9A04C1CB6 CRC64;
MDDELRDRIT EAAETNALLN AVKHDSEAQV GAIMGPLMGE NPEFREYGDE IPGVIAPVVE
RVNGMDAEER RERLAELAPE KLEELEAEDE GEDHPLPDLP SAEEYDTVRM RVAPNPNGPW
HIGHARMAAV VGTYKQRYDG EFICRFDDTD PETKRPDLDA YDAILDAIDY LGFEPDDVVN
ASDRVETYYE YARKLIDKGG AYTCSCPQGE FSDLKNNGEA CPHRDKDAET TRSEFEAMVD
GEYDSGEMVL RVRTDITHKN PALRDFVAFR MVDTPHPREA AEQYRCWPML DFQSGLDDHL
LGVTHIIRGI DLQDSAKRQQ FVYDYFDWEY PEVIHWGHVQ VDEYDVPLST SSIAELIEDG
ELAGWDDPRA PTVASLERRG IRGEAVVDAM IQLGTSTSNV DLAMSSIYSN NRDLIDDDSD
RAFFVRDSDD HGGLVERQIV GGPDAGEPPL HPDYEERGRR EIPVTSGVVV EGDDLPDHGD
RIWLKGYGCV RHTRDAFEYT GDDIDAVREE GVDVIHWAPA DGPALRLRTM DGDVSGVAEP
GLRNYDTDDV VQFERIGFAR LDKVADDSDT ESVAYFTHP