SYGB_XANCB
ID SYGB_XANCB Reviewed; 698 AA.
AC B0RYX3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=xcc-b100_4289;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; AM920689; CAP53659.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RYX3; -.
DR SMR; B0RYX3; -.
DR KEGG; xca:xcc-b100_4289; -.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000001188; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SMART; SM00836; DALR_1; 1.
DR TIGRFAMs; TIGR00211; glyS; 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..698
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101371"
SQ SEQUENCE 698 AA; 75049 MW; 3DF69C48AB136303 CRC64;
MSEQLPLLIE LGTEELPVKA LPGLAQAFFD GVLAGLEKRG VAVTRGDAKP LSTPRRLAVL
LPGVATEQPE QRSEVLGPYL NIALDAEGKP TRALAGFAAK AGIDWTALER TSDAKGERFV
HRAVTPGAQA AALLPEILRE AIAAMPIPKP MRWGAHEYAF ARPVQWLVLL FGDTVIPAEL
LGVRGDRITR GHRFMHDGDI ALAAPGDYID ALRAAHVLVD ADARRARIVE EVDAAARQAG
GSARISDDNL EQVVNLVEWP SAVLCSFERA FLAVPQEALI ETMEINQKFF PVLDDGGKLT
EQFIGIANIV SKDVAEVAKG YERVIRPRFA DAKFFFDEDL KQGLEAMGAG LASVTYQAKL
GTVADKVARV AALAEAIAPQ VGADPVQARR AAELAKNDLQ SRMVNEFPEL QGIAGRHYAK
AAGEPSEISL AIDEAYQPRF AGDDIALSPL GKVLAIAERL DTLAGGFAAG LKPTGNKDPF
ALRRNALGLA RTVIESGFDL DLPKLIDVGL ASLPDAVKPH ADRNTETVRA DLYDFILDRL
KGYYADKGVA ATHFNAVAEL TPASLYDFDR RIDAIGIFAT LPEAEALAAA NKRIRNILRK
VEGEIPGDID TTLLREPAEE ALAEAVEAAI GDTGDALHRH DYVAVLARLA RLRPQVDAFF
DGVMVNADDP QLRANRLALL KKLGDRLGSV AAIEHLSS