ID   SYG_CLOTE               Reviewed;         463 AA.
AC   Q899G6;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253};
DE   AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253};
GN   Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; OrderedLocusNames=CTC_00212;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC   -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC       {ECO:0000255|HAMAP-Rule:MF_00253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000255|HAMAP-Rule:MF_00253};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR   EMBL; AE015927; AAO34860.1; -; Genomic_DNA.
DR   RefSeq; WP_011098530.1; NC_004557.1.
DR   AlphaFoldDB; Q899G6; -.
DR   SMR; Q899G6; -.
DR   STRING; 212717.CTC_00212; -.
DR   EnsemblBacteria; AAO34860; AAO34860; CTC_00212.
DR   GeneID; 64181009; -.
DR   KEGG; ctc:CTC_00212; -.
DR   HOGENOM; CLU_015515_2_1_9; -.
DR   OMA; EPSYGID; -.
DR   OrthoDB; 626850at2; -.
DR   Proteomes; UP000001412; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00774; GlyRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR   InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR   InterPro; IPR033731; GlyRS-like_core.
DR   InterPro; IPR002315; tRNA-synt_gly.
DR   PANTHER; PTHR10745; PTHR10745; 3.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01043; TRNASYNTHGLY.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..463
FT                   /note="Glycine--tRNA ligase"
FT                   /id="PRO_0000072954"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         207..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         217..222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         222..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         291..292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         331..335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT   BINDING         335..338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ   SEQUENCE   463 AA;  53718 MW;  3A4AD370E09C47AF CRC64;
     MTVEKTMDKI VALAKNRGFI FPGSEIYGGL ANSWDYGPLG VEFKNNVKKA WWKKFVQESP
     YNVGIDAAIL MNREVWVASG HVGGFSDPLM DCKECKARCR ADKLIEDYMQ DKDENFESAD
     GWSNEQLKDF IDKNNIACPK CGEHNFTDVR KFNLMFKTFQ GVTEDAQSEI FLRPETAQGI
     FVNFKNAIRT TRRKMPFGMA QIGKSFRNEI TPGNFTFRTR EFEQMELEFF CKPGTDLEWF
     EYWRDYSWNF LLSLGLAKDN LRIREHAKEE LAFYSKATVD IEYLFPFGWG ELWGIADRTD
     YDLKQHMNHS GKDLTYLDPE TNEKYLPYCI EPSLGADRVA LAFLVDAYDE EELDGGDSRT
     VLRLHPALAP FKAAILPLTK KLKDKSLEVY SMLSKYFNVD YDEAGTIGKR YRREDEIGTP
     YCITIDYDTL EDNTVTIRDR DSMDQIRINI DELVKYISEK VEF