ID   SYGA_BRAHW              Reviewed;         290 AA.
AC   C0R0J6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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}; OrderedLocusNames=BHWA1_01154;
OS   Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=565034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49526 / WA1;
RX   PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA   Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA   Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA   Barrero R., Phillips N.D., Hampson D.J.;
RT   "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT   hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT   intestine.";
RL   PLoS ONE 4:E4641-E4641(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; CP001357; ACN83634.1; -; Genomic_DNA.
DR   RefSeq; WP_012670681.1; NC_012225.1.
DR   AlphaFoldDB; C0R0J6; -.
DR   SMR; C0R0J6; -.
DR   STRING; 565034.BHWA1_01154; -.
DR   EnsemblBacteria; ACN83634; ACN83634; BHWA1_01154.
DR   KEGG; bhy:BHWA1_01154; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_12; -.
DR   OMA; SYYQFQV; -.
DR   Proteomes; UP000001803; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..290
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000125536"
SQ   SEQUENCE   290 AA;  33451 MW;  5761051D4BDE0B9C CRC64;
     MTFTDLIMTL NKFWSENGCI IQQGYDLEVG AGTFNPATAL RALGPEPFSV AYVEPSRRPT
     DGRYGENPNR LQHYYQYQVI MKPSPENIQD LYIQSLEALG ISFKDHDIRF VHDDWESPTL
     GAWGLGWEVW LDGMEITQFT YFQAVGGINL KPITGEITYG LERICMYLQN IDNVYDLEWG
     HGIKYGDVHL QGEKEFSKYN FEVADTDMYF RHFKEYEEEC DRCLANGCVL PAYDMVMKSS
     HVFNMLDARN AISVTERAGY IARVRELMKK VSAAYIESRE KLGYPLIKNK