ID   SYE_SACS2               Reviewed;         575 AA.
AC   P95968;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 134.
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};
GN   OrderedLocusNames=SSO0093; ORFNames=C04029, C05_017;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA   Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA   Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA   Ragan M.A., Charlebois R.L.;
RT   "Organizational characteristics and information content of an archaeal
RT   genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL   Mol. Microbiol. 22:175-191(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; Y08257; CAA69558.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK40450.1; -; Genomic_DNA.
DR   PIR; S75395; S75395.
DR   AlphaFoldDB; P95968; -.
DR   SMR; P95968; -.
DR   STRING; 273057.SSO0093; -.
DR   PaxDb; 273057-SSO0093; -.
DR   EnsemblBacteria; AAK40450; AAK40450; SSO0093.
DR   KEGG; sso:SSO0093; -.
DR   PATRIC; fig|273057.12.peg.90; -.
DR   eggNOG; arCOG04302; Archaea.
DR   HOGENOM; CLU_001882_1_3_2; -.
DR   InParanoid; P95968; -.
DR   PhylomeDB; P95968; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0043604; P:amide biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd09287; GluRS_non_core; 1.
DR   Gene3D; 2.40.240.100; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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_bL25/Gln-tRNA_synth_N.
DR   InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR049437; tRNA-synt_1c_C2.
DR   NCBIfam; TIGR00463; gltX_arch; 1.
DR   PANTHER; PTHR43097:SF4; GLUTAMINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43097; GLUTAMINE-TRNA LIGASE; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF20974; tRNA-synt_1c_C2; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..575
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000119731"
FT   MOTIF           108..118
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
SQ   SEQUENCE   575 AA;  66805 MW;  150D562D4BFED19E CRC64;
     MMELNELRET IYKYALQNAV KHNGKAETGP VMSKIIAERP ELRSNAREIV KIIKEIIEQV
     NSLTLEQQLT EIKAKYPELL EEKKHEEKRK VLPPLPNVKG QVVTRFAPNP DGPLHLGNAR
     SAILSYEYAK MYNGKFILRF DDTDPKVKRP ILDAYDWIKE DLKWLGIKWE QELYASERLE
     LYYKYARYLI EKGYAYVDTC DSSIFRKFRD SRGKMKEPEC LHRSSSPESN LELFEKMLGG
     KFKEGEAVVR LKTDLSDPDP SQIDWVMLRI IDTAKNPHPR VGSKYWVWPT YNFASIIDDH
     ELGITHVLRA KEHMSNTEKQ RYISEYMGWE FPEVLQFGRL RLEGFMMSKS KIRGMLEKGT
     NRDDPRLPTL AGLRRRGILP DTIKDVIIDV GVKVTDATIS FENIAAINRK KLDPVAKRIM
     FVKDAEEFSV ELPESLNAKI PLIPSKQEMN RTIIVNPGDK ILIESNDAED NSILRLMELC
     NVKVDKHNRK LIFHSKTLDE AKKVNAKIVQ WVKSNEKVPV MVEKAERDEI KMINGYAEKI
     AADLEIDEIV QFYRFGFVRV DRKDENMLRV VFSHD
//