SYG_THET8
ID SYG_THET8 Reviewed; 506 AA.
AC P56206; O50551; Q5SKV0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glycine--tRNA ligase;
DE EC=6.1.1.14 {ECO:0000269|PubMed:9490048, ECO:0000305|PubMed:10064708};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000303|PubMed:7556056};
DE Short=GlyRS {ECO:0000303|PubMed:7556056};
GN Name=glyQS; Synonyms=glyS {ECO:0000303|PubMed:9490048};
GN OrderedLocusNames=TTHA0543;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1] {ECO:0007744|PDB:1ATI}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS)
RP OF 3-506, AND SUBUNIT.
RX PubMed=7556056; DOI=10.1002/j.1460-2075.1995.tb00089.x;
RA Logan D.T., Mazauric M.-H., Kern D., Moras D.;
RT "Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.";
RL EMBO J. 14:4156-4167(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9490048; DOI=10.1046/j.1432-1327.1998.2510744.x;
RA Mazauric M.-H., Keith G., Logan D., Kreutzer R., Giege R., Kern D.;
RT "Glycyl-tRNA synthetase from Thermus thermophilus -- wide structural
RT divergence with other prokaryotic glycyl-tRNA synthetases and functional
RT inter-relation with prokaryotic and eukaryotic glycylation systems.";
RL Eur. J. Biochem. 251:744-757(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:1B76, ECO:0007744|PDB:1GGM}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-506 IN COMPLEX WITH ATP AND
RP SUBSTRATE ANALOG, AND SUBUNIT.
RX PubMed=10064708; DOI=10.1006/jmbi.1999.2562;
RA Arnez J.G., Dock-Bregeon A.-C., Moras D.;
RT "Glycyl-tRNA synthetase uses a negatively charged pit for specific
RT recognition and activation of glycine.";
RL J. Mol. Biol. 286:1449-1459(1999).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000269|PubMed:9490048}.
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:0000269|PubMed:9490048,
CC ECO:0000305|PubMed:10064708};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10064708,
CC ECO:0000269|PubMed:7556056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ222643; CAA10903.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70366.1; -; Genomic_DNA.
DR RefSeq; WP_011228014.1; NC_006461.1.
DR RefSeq; YP_143809.1; NC_006461.1.
DR PDB; 1ATI; X-ray; 2.75 A; A/B=3-506.
DR PDB; 1B76; X-ray; 3.40 A; A/B=3-506.
DR PDB; 1GGM; X-ray; 3.40 A; A/B=3-506.
DR PDBsum; 1ATI; -.
DR PDBsum; 1B76; -.
DR PDBsum; 1GGM; -.
DR AlphaFoldDB; P56206; -.
DR SMR; P56206; -.
DR STRING; 300852.55771925; -.
DR EnsemblBacteria; BAD70366; BAD70366; BAD70366.
DR GeneID; 3169948; -.
DR KEGG; ttj:TTHA0543; -.
DR PATRIC; fig|300852.9.peg.542; -.
DR eggNOG; COG0423; Bacteria.
DR HOGENOM; CLU_015515_2_1_0; -.
DR OMA; EPSYGID; -.
DR PhylomeDB; P56206; -.
DR BRENDA; 6.1.1.14; 2305.
DR EvolutionaryTrace; P56206; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0009345; C:glycine-tRNA ligase complex; IDA:CAFA.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0016594; F:glycine binding; IDA:CAFA.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IDA:CAFA.
DR CDD; cd00774; GlyRS-like_core; 1.
DR DisProt; DP00032; -.
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 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..506
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000072983"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="substrate"
FT BINDING 221..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10064708"
FT BINDING 231..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10064708"
FT BINDING 236..240
FT /ligand="substrate"
FT BINDING 305..306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10064708"
FT BINDING 360..364
FT /ligand="substrate"
FT BINDING 364..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:10064708"
FT CONFLICT 2
FT /note="P -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 116..120
FT /note="YRAME -> TGPWR (in Ref. 2; CAA10903)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..182
FT /note="KTYVGPVEDEAS -> QDLRGPRGGRGL (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..200
FT /note="QGIFVNFKN -> RASSSTSRT (in Ref. 2; CAA10903)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="P -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..220
FT /note="IGKAF -> SARPS (in Ref. 2; CAA10903)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="E -> R (in Ref. 2; CAA10903)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..285
FT /note="EL -> SS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 303..304
FT /note="LE -> SL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="N -> Q (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 37..54
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:1B76"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 209..221
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 234..245
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:1ATI"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 315..320
FT /evidence="ECO:0007829|PDB:1ATI"
FT TURN 324..328
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:1ATI"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:1GGM"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 412..426
FT /evidence="ECO:0007829|PDB:1ATI"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:1B76"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:1ATI"
FT TURN 473..476
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:1ATI"
FT TURN 483..485
FT /evidence="ECO:0007829|PDB:1ATI"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:1ATI"
FT HELIX 493..504
FT /evidence="ECO:0007829|PDB:1ATI"
SQ SEQUENCE 506 AA; 58387 MW; C0794381A539FD89 CRC64;
MPASSLDELV ALCKRRGFIF QSSEIYGGLQ GVYDYGPLGV ELKNNLKQAW WRRNVYERDD
MEGLDASVLT HRLVLHYSGH EATFADPMVD NRITKKRYRL DHLLKEQPEE VLKRLYRAME
VEEENLHALV QAMMQAPERA GGAMTAAGVL DPASGEPGDW TPPRYFNMMF KTYVGPVEDE
ASLAYLRPET AQGIFVNFKN VLDATSRKLP FGIAQIGKAF RNEITPRNFI FRVREFEQME
IEYFVRPGED EYWHRYWVEE RLKWWQEMGL SRENLVPYQQ PPEELAHYAK ATVDILYRFP
HGLEELEGIA NRTDFDLGSH TKDQEALGIT ARVLRNEHST QRLAYRDPET GKWFVPYVIE
PSAGVDRGVL ALLAEAFTRE ELPNGEERIV LKLKPQLAPI KVAVIPLVKN RPEITEYAKR
LKARLLALGL GRVLYEDTGN IGKAYRRHDE VGTPFAVTVD YDTIGQSKDG TTRLKDTVTV
RDRDTMEQIR LHVDELEGFL RERLRW
