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SYE2_SULDN
ID   SYE2_SULDN              Reviewed;         432 AA.
AC   Q30RP4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Glutamate--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS 2 {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX2 {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=Suden_1059;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Thiovulaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
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_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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00022};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
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DR   EMBL; CP000153; ABB44337.1; -; Genomic_DNA.
DR   RefSeq; WP_011372689.1; NC_007575.1.
DR   AlphaFoldDB; Q30RP4; -.
DR   SMR; Q30RP4; -.
DR   STRING; 326298.Suden_1059; -.
DR   PRIDE; Q30RP4; -.
DR   EnsemblBacteria; ABB44337; ABB44337; Suden_1059.
DR   KEGG; tdn:Suden_1059; -.
DR   eggNOG; COG0008; Bacteria.
DR   HOGENOM; CLU_015768_6_0_7; -.
DR   OMA; NFACACD; -.
DR   OrthoDB; 1409413at2; -.
DR   Proteomes; UP000002714; 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:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; -; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; SSF48163; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 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..432
FT                   /note="Glutamate--tRNA ligase 2"
FT                   /id="PRO_0000367777"
FT   MOTIF           6..16
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           235..239
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   432 AA;  49972 MW;  E6E7129BB0460582 CRC64;
     MLRFAPSPTG DMHIGNLRVA IFNYIVSKQR KEDLVIRIED TDKDRNIEGK DKEILDILNL
     FGIDYSVVMY QSENFRFHRA MALQLLQDKR AFNCFCSSDW LDKKREEAKN SKTAYRYDDA
     CASLPDELVI DNEHPFTVRI RKPLEPIIIK DHIKGEIKFE PNDIDSFIIM RQDKTPMYNF
     ACAVDDMLSD ISLVIRGEDH VSNTPKQILI REALGYSKNI EYAHLPIILN DDGKKMSKRD
     DASSVKWLLE EGYLPSAIAN YLILIGNKPP KEIFTIQEAI EWFSLENISK SPARFDINML
     KHVNKEHLKI LDAKELSRYV GFADAQIGEV AKIYLEEAST TKELRAKIAL IFAEKNIPDE
     FKEYAQTIVK IIQKAPYFEE YEDFKNYIIQ ESGLKGKNFF KPLRILLMGS EHGPDIATVY
     KHIKNYLGEI VK
 
 
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