ID   SYGA_BUCAT              Reviewed;         312 AA.
AC   B8D741;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254};
GN   OrderedLocusNames=BUAPTUC7_135;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=561501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuc7;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
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DR   EMBL; CP001158; ACL29956.1; -; Genomic_DNA.
DR   RefSeq; WP_009874092.1; NC_011834.1.
DR   AlphaFoldDB; B8D741; -.
DR   SMR; B8D741; -.
DR   KEGG; bau:BUAPTUC7_135; -.
DR   HOGENOM; CLU_057066_1_0_6; -.
DR   OMA; SYYQFQV; -.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..312
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000125540"
SQ   SEQUENCE   312 AA;  36961 MW;  A138A9BEBC6CE8C6 CRC64;
     MKNYHNNFHK LITILQEYWL QQGCTIFQPL DLPIGAGTFH NITFLGTIGP EPINAAYIQS
     CRRPSDGRYG ENPNRLQHYY QFQVIIKPPP NNIQNIYLNS LYLLNIDEKI HDIRFVEDNW
     ENPTLGAWGI GWEVWLNGME ITQFTYFQQV GGLECKPVSV EITYGLERIA MHMQNKSNVY
     DLIWNEYNHK KITYGDIFQQ NEREQSQYNF QYSDVNFLFD CFKKYELEAK KLINLKEPLL
     LVSYEKILQA NHIFNLLDAR KSLSSNERQS YILRIRKLTS QVAIKYLNLR KNLGFPLCHK
     KREIHDKENI IN