ID   SYEC_ENTBH              Reviewed;         631 AA.
AC   A9CSZ1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Probable glutamate--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
DE            Short=GluRS;
GN   ORFNames=EBI_22577;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA   Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(2009).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 2 subfamily. {ECO:0000305}.
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DR   EMBL; ABGB01000003; EDQ31175.1; -; Genomic_DNA.
DR   RefSeq; XP_001828010.1; XM_001827958.1.
DR   AlphaFoldDB; A9CSZ1; -.
DR   SMR; A9CSZ1; -.
DR   STRING; 481877.A9CSZ1; -.
DR   VEuPathDB; MicrosporidiaDB:EBI_22577; -.
DR   HOGENOM; CLU_001882_1_2_1; -.
DR   InParanoid; A9CSZ1; -.
DR   OMA; ANRYFFV; -.
DR   OrthoDB; 934at2759; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; IPR020061; Glu_tRNA_lig_a-bdl.
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   PANTHER; PTHR43097:SF5; GLUTAMATE--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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..631
FT                   /note="Probable glutamate--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000388392"
FT   MOTIF           144..153
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           367..371
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..141
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         311..315
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         367..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   631 AA;  73962 MW;  4DC6852631BEA04D CRC64;
     MLENISKSEF VNFLLEKKHN IEPKTLPILE QHIREQKLDD FFLDFSIDFT DEELNNFLSK
     LDYWLKNTKL NSSKADVIFG LLYSCNKFIK LIKNPTFSFV EIKQFYNDIL NTNKNYIIEY
     NKKDKGKINI AVEGNVVTRF PPEPSGFLHI GHIKAALLND LMAKNGKLLI RFDDTNPIKE
     EKMYENVIIE DLHTLGIKNY TIVRSSDHFD SLYNYAIQLI QLGLAYCDNT DQLQMREERT
     KGIPSKNRNT DIETNLSIFS KMSSGNCLDY CLRAKIDYTN LNKALRDPVI YRHIEKEHNI
     TKNKYKIYPT YDFACPIIDS LDGVTLALRT NEYRDRNEQY YWFLEKLNLP NKPKIYDFSR
     LNFENTVLSK RQMKFYVDNH FVSGWDDPRL STLRGILRLG MDIDTLKEYI INQGSSQKSS
     VISWDKVWSL NKKNIDHKSA RYSAIPKLYC VECLILDKNN NEIITKTEDI PKFKKNLSLG
     NKTIIKSSHI LISQEDANIL NNNEEFTLMN WGNMKVKEKQ IVNGIIIKII LEENLAGDVK
     TTKNKLTWVN KENIIEFKIL EYDTLQNDKN TDNLAEKFNT NSKKEEIWLG EKALISVSPK
     TYIQIERIGF FICDKPLEFI LIPYTKQKRM R
//