SYGA_ECOLI
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 03-AUG-2022, entry version 175.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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;
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}.
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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_CP064683.1.
DR PDB; 7EIV; X-ray; 2.68 A; A/B=1-303.
DR PDBsum; 7EIV; -.
DR AlphaFoldDB; P00960; -.
DR SMR; P00960; -.
DR BioGRID; 4259717; 48.
DR BioGRID; 852387; 7.
DR ComplexPortal; CPX-5201; Glycyl-tRNA synthetase complex.
DR DIP; DIP-9816N; -.
DR IntAct; P00960; 33.
DR STRING; 511145.b3560; -.
DR jPOST; P00960; -.
DR PaxDb; P00960; -.
DR PRIDE; P00960; -.
DR EnsemblBacteria; AAC76584; AAC76584; b3560.
DR EnsemblBacteria; BAE77734; BAE77734; BAE77734.
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-MON; -.
DR BioCyc; MetaCyc:GLYQ-MON; -.
DR PRO; PR:P00960; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009345; C:glycine-tRNA ligase complex; IPI:ComplexPortal.
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 Gene3D; 3.30.930.10; -; 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 Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00388; glyQ; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 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 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 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 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..212
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
