SYGA_XANC5
ID SYGA_XANC5 Reviewed; 302 AA.
AC Q3BMH1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=XCV4311;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ26042.1; -; Genomic_DNA.
DR RefSeq; WP_008577775.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BMH1; -.
DR SMR; Q3BMH1; -.
DR STRING; 456327.BJD11_23835; -.
DR EnsemblBacteria; CAJ26042; CAJ26042; XCV4311.
DR GeneID; 63993357; -.
DR KEGG; xcv:XCV4311; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_6; -.
DR OMA; SYYQFQV; -.
DR Proteomes; UP000007069; 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..302
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_1000047529"
SQ SEQUENCE 302 AA; 34362 MW; 72CE1CC1318A1AE2 CRC64;
MSDSRRVPIT FQGLIQTLNQ YWAEQGCVLI QPLDLEVGAG TFHPATFLRA LGPEPWNAAY
VQPSRRPTDG RYGENPNRLQ RYYQYQVAMK PNPDNIQDLY LGSLQALGID PLVHDLRFVE
DNWESPTLGA WGLGWEVWLN GMEVTQFTYF QQAGGLECKP VLGEITYGLE RLCMYLQSCD
NVYELVWTYG PDGAAVTYGD VYHQNEVEQS TYNFEHANVA ELFHRFDACE AEARHLVEVG
LPLPAYEQVT KASHAFNLLD ARRAISVTER QRYILRVRAL AQGVAQAYYA QREKLGFPGV
KK