SYG_METTP
ID SYG_METTP Reviewed; 577 AA.
AC A0B5U4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=glyS {ECO:0000255|HAMAP-Rule:MF_00253}; OrderedLocusNames=Mthe_0271;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR EMBL; CP000477; ABK14068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B5U4; -.
DR SMR; A0B5U4; -.
DR STRING; 349307.Mthe_0271; -.
DR EnsemblBacteria; ABK14068; ABK14068; Mthe_0271.
DR KEGG; mtp:Mthe_0271; -.
DR HOGENOM; CLU_015515_1_2_2; -.
DR OMA; EPSYGID; -.
DR Proteomes; UP000000674; 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_A; Gly_tRNA_synth_A; 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; IPR022960; Gly_tRNA_ligase_arc.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR PANTHER; PTHR10745; PTHR10745; 1.
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..577
FT /note="Glycine--tRNA ligase"
FT /id="PRO_1000047379"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 193..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 203..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 208..212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 319..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 430..434
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 434..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 577 AA; 66541 MW; 3E0E87B905AECCE5 CRC64;
MDRYEQVTEL ARRRGFMWPS FELYGGAAGF YDYGPLGARL KRRIEDIWRR FFVIGEGFAE
IECPTIGIEE VFRASGHLSG FSDPLTECKE CKEIYRADHL IKHIVEVPDA LSAEEIYRMI
KENDITCPEC GGELSEVYEF NLMFRTAIGP GNRHPGYLRP ETAQGMFINF QRLLRYYRDS
LPFGAVQIGR SYRNEISPRQ GVIRLREFSQ AEAEVFIDPR NKQHPRFSEV KDLRLRLYSR
EAQERGQVEE MSVGEAVERG IIAHEILAYF VARTYEYLLA VGVDRERLRF RQHKADEMAH
YAADCWDAEV LLDRLGWIEI VGIADRTDYD LRSHMALSKA NLSVFVHYPE PVRRKRVAVK
PDMKVLGPRF KGRAKAIADA LQAMSVADLK GDTIKITVDG ETYEIERRLV SVEEIEEEIR
GEYVVPHVIE PSFGIDRILY TVLEHSYHEE PVEDEMRVVL RFLPGISPID VAILPLMDKD
ELVEPARRIF DEFRRCGMLA EFDTSGSIGR RYRRNDEIGT PYCITVDYQT LEDGTVTVRD
RDTMQQIRIE ADRAVDIIRD LMSGALCFSE AGMPVKS
