ID SYGA_ECOLI Reviewed; 303 AA. AC P00960; Q2M7M2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 2. DT 10-JUN-2026, entry version 189. DE RecName: Full=Glycine--tRNA ligase alpha subunit; DE EC=6.1.1.14; DE AltName: Full=Glycyl-tRNA synthetase alpha subunit; DE Short=GlyRS; GN Name=glyQ; Synonyms=glyS(A); OrderedLocusNames=b3560, JW3531; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6309809; DOI=10.1016/s0021-9258(17)44504-2; RA Webster T.A., Gibson B.W., Keng T., Biemann K., Schimmel P.; RT "Primary structures of both subunits of Escherichia coli glycyl-tRNA RT synthetase."; RL J. Biol. Chem. 258:10637-10641(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region RT from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 268-303. RX PubMed=6290471; DOI=10.1016/s0021-9258(18)33539-7; RA Keng T., Webster T.A., Sauer R.T., Schimmel P.; RT "Gene for Escherichia coli glycyl-tRNA synthetase has tandem subunit coding RT regions in the same reading frame."; RL J. Biol. Chem. 257:12503-12508(1982). CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Gly) + glycine + ATP = glycyl-tRNA(Gly) + AMP + CC diphosphate; 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; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC -!- INTERACTION: CC P00960; P00961: glyS; NbExp=3; IntAct=EBI-551191, EBI-551400; CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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; J01622; AAA23914.1; -; Genomic_DNA. DR EMBL; U00039; AAB18537.1; -; Genomic_DNA. DR EMBL; U00096; AAC76584.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77734.1; -; Genomic_DNA. DR EMBL; J01623; AAA23916.1; -; Genomic_DNA. DR PIR; B65155; SYECGA. DR RefSeq; NP_418017.1; NC_000913.3. DR RefSeq; WP_001168560.1; NZ_CP064677.1. DR PDB; 7EIV; X-ray; 2.68 A; A/B=1-303. DR PDB; 7QCF; X-ray; 3.00 A; A/B/C/D=2-303. DR PDB; 7YSE; X-ray; 2.91 A; A/B=1-303. DR AlphaFoldDB; P00960; -. DR SMR; P00960; -. DR BioGRID; 4259717; 52. DR BioGRID; 852387; 7. DR ComplexPortal; CPX-5201; Glycyl-tRNA synthetase complex. DR DIP; DIP-9816N; -. DR FunCoup; P00960; 520. DR IntAct; P00960; 33. DR STRING; 511145.b3560; -. DR jPOST; P00960; -. DR PaxDb; 511145-b3560; -. DR EnsemblBacteria; AAC76584; AAC76584; b3560. DR GeneID; 948079; -. DR KEGG; ecj:JW3531; -. DR KEGG; eco:b3560; -. DR PATRIC; fig|511145.12.peg.3674; -. DR EchoBASE; EB0404; -. DR eggNOG; COG0752; Bacteria. DR HOGENOM; CLU_057066_1_0_6; -. DR InParanoid; P00960; -. DR PhylomeDB; P00960; -. DR BioCyc; EcoCyc:GLYQ-MONOMER; -. DR BioCyc; MetaCyc:GLYQ-MONOMER; -. DR PRO; PR:P00960; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P00960; -. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0009345; C:glycine-tRNA ligase complex; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IDA:ComplexPortal. DR CDD; cd00733; GlyRS_alpha_core; 1. DR FunFam; 1.20.58.180:FF:000001; Glycine--tRNA ligase alpha subunit; 1. DR FunFam; 3.30.930.10:FF:000006; Glycine--tRNA ligase alpha subunit; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 1.20.58.180; Class II aaRS and biotin synthetases, domain 2; 1. DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer. DR InterPro; IPR002310; Gly-tRNA_ligase_asu. DR NCBIfam; TIGR00388; glyQ; 1. DR NCBIfam; NF006827; PRK09348.1; 1. DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1. DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1. DR Pfam; PF02091; tRNA-synt_2e; 1. DR PRINTS; PR01044; TRNASYNTHGA. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. DR PDBsum; 7EIV; -. DR PDBsum; 7QCF; -. DR PDBsum; 7YSE; -. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..303 FT /note="Glycine--tRNA ligase alpha subunit" FT /id="PRO_0000072836" FT CONFLICT 48 FT /note="E -> A (in Ref. 1; AAA23914)" FT /evidence="ECO:0000305" FT CONFLICT 65 FT /note="P -> A (in Ref. 1; AAA23914)" FT /evidence="ECO:0000305" FT HELIX 9..21 FT /evidence="ECO:0007829|PDB:7EIV" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:7YSE" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:7EIV" FT TURN 46..48 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 54..63 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 78..89 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 94..104 FT /evidence="ECO:0007829|PDB:7EIV" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:7QCF" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 128..137 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 140..151 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 154..166 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 167..175 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 195..208 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 209..213 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 216..234 FT /evidence="ECO:0007829|PDB:7EIV" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 241..260 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 266..293 FT /evidence="ECO:0007829|PDB:7EIV" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:7EIV" SQ SEQUENCE 303 AA; 34774 MW; 91E20623ADFD4DDB CRC64; MQKFDTRTFQ GLILTLQDYW ARQGCTIVQP LDMEVGAGTS HPMTCLRELG PEPMAAAYVQ PSRRPTDGRY GENPNRLQHY YQFQVVIKPS PDNIQELYLG SLKELGMDPT IHDIRFVEDN WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGLERL AMYIQGVDSV YDLVWSDGPL GKTTYGDVFH QNEVEQSTYN FEYADVDFLF TCFEQYEKEA QQLLALENPL PLPAYERILK AAHSFNLLDA RKAISVTERQ RYILRIRTLT KAVAEAYYAS REALGFPMCN KDK //