SYE_PYRAB
ID SYE_PYRAB Reviewed; 571 AA.
AC Q9V1E3; G8ZGI9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
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=PYRAB04840;
GN ORFNames=PAB0323;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(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: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; AJ248284; CAB49406.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69868.1; -; Genomic_DNA.
DR PIR; G75165; G75165.
DR RefSeq; WP_010867608.1; NC_000868.1.
DR AlphaFoldDB; Q9V1E3; -.
DR SMR; Q9V1E3; -.
DR STRING; 272844.PAB0323; -.
DR EnsemblBacteria; CAB49406; CAB49406; PAB0323.
DR GeneID; 1495381; -.
DR KEGG; pab:PAB0323; -.
DR PATRIC; fig|272844.11.peg.512; -.
DR eggNOG; arCOG04302; Archaea.
DR HOGENOM; CLU_001882_1_3_2; -.
DR OMA; MRFAPNP; -.
DR OrthoDB; 8922at2157; -.
DR PhylomeDB; Q9V1E3; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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: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 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.
FT CHAIN 1..571
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119725"
FT MOTIF 106..116
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ SEQUENCE 571 AA; 65920 MW; D7BA5D954B1A8AC6 CRC64;
MEVERIALKY ALINAIEHGG KANPKAVIGK VLGENPELRS KAREIVPIIN KVVEEVNSLS
LDEQKAKLME IYPEYFEKKE EKKEEKKGLP PLPKAEKGKV VTRFAPNPDG AFHLGNARAA
ILSYEYAKMY GGKFILRFDD TDPKVKRPEP IFYEMIIEDL EWLGIKPDEI VYASDRLELY
YKYAEELIKM GKAYVCTCKP EKFRELRDKG IPCPHRDEPV EVQLERWRKM LNGEYKEGEA
VVRIKTDLNH PNPAVRDWPA LRIVDNPNHP RAGNKYRVWP LYNFASAIDD HELGVTHIFR
GQEHAENETR QRYIYEYFGW EYPVTVHHGR LSIEGVILSK SKTRKGIEEG KYLGWDDPRL
GTIRALRRRG ILPEAIKELI IEVGLKKSDA TVSWDNLAAI NRKLVDPIAN RYFFVADPVP
MEVEGAPEFI AKIPLHPDHP ERGTRELRFT PGKPIYVSKD DLDLLKPGSF VRLKDLFNVE
IVEVGEKIKA KFHSFEYEIA RKNKWRMIHW VPEGRPCEVI IPEGDELIVR KGLLEKDANV
KAGEIVQFER FGFVRIDKIE GEKVVAIYAH K
