SYG_COREF
ID SYG_COREF Reviewed; 461 AA.
AC Q8FNG6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=CE2178;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC18988.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC18988.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006768181.1; NZ_GG700683.1.
DR AlphaFoldDB; Q8FNG6; -.
DR SMR; Q8FNG6; -.
DR STRING; 196164.23494020; -.
DR PRIDE; Q8FNG6; -.
DR EnsemblBacteria; BAC18988; BAC18988; BAC18988.
DR KEGG; cef:CE2178; -.
DR eggNOG; COG0423; Bacteria.
DR HOGENOM; CLU_015515_2_1_11; -.
DR OrthoDB; 626850at2; -.
DR Proteomes; UP000001409; 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..461
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000072955"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 195..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 205..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 210..214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 282..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 322..326
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 326..329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 461 AA; 52831 MW; EC990D59283637F2 CRC64;
MAQQSIIDTV VNLCKRRGLV YPCGEIYGGT RSAWDYGPLG VELKENIKRQ WWRTMVTSRP
DVVGVDTSVI LPRQVWVTSG HVEVFTDPLV ESLHTHKRYR ADHLLEAYEE KHGHPPANGL
ADINDPETGQ PGKWTEPKAF SGLLKTFLGP VDDEEGLHYL RPETAQGIFV NFKNVMNSSR
MKPPFGIANI GKSFRNEITP GNFIFRTREF EQMEMEFFVK PGEDEEWHQH WIDARHQWYI
DLGVNPDNLR LYEHPQEKLS HYSKRTVDIE YAFNFANSKW GELEGIANRT DYDLRVHSEG
SGEDLSYFDQ ETGERWIPYV IEPAAGLGRA MMVFLMDAYH EDEAPNSKGG VDKRVVLKLD
RRLAPVKVAV LPLSKKPELS GPAEKLAAEL RQFWNVEYDT SGAIGRRYRR QDEIGTPFCV
TVDFDTLEDN AVTVRERDTM EQIRVPLDEL QGYLAQQLIG C
