SYGB_THIDA
ID SYGB_THIDA Reviewed; 701 AA.
AC Q3SGF0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
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}; OrderedLocusNames=Tbd_2347;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ98300.1; -; Genomic_DNA.
DR RefSeq; WP_011312859.1; NC_007404.1.
DR AlphaFoldDB; Q3SGF0; -.
DR SMR; Q3SGF0; -.
DR STRING; 292415.Tbd_2347; -.
DR EnsemblBacteria; AAZ98300; AAZ98300; Tbd_2347.
DR KEGG; tbd:Tbd_2347; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000008291; 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 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; Reference proteome.
FT CHAIN 1..701
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101367"
SQ SEQUENCE 701 AA; 74976 MW; 7AB01C1B158AD320 CRC64;
MTTANLLVEL FVEELPPKAL KKLGEAFAAA LTESLVAQGL VHAQAAVTHF ASPRRLGAHI
ENVLERSADK PVSTKLMPVS VGLDADGNAT PALLKRLAAL GADASAVATL RRESDGKAEA
LFMDSVAKGI SLGLGLAKAL WESLDKLPIP KVMSYQLADG WSTVNFVRPV HGLVALHGTD
PVDVRMFGLT AGRKTHGHRF EAAADPIVLK DADSYAQQLE SEGAVIANFA ERRAEIVRQL
EAAAAPLGLV PVEDEALLDE VTALVERPNV LLGQFEQAFL EVPQECLILT MKANQKYFPL
LDAAGKLTNK FLIVSNISPA DASAVVGGNE RVVRPRLADA KFFFDQDRKK TLDARVLGLA
KVVYHNKLGT QGERVTRVQA VARAIGEKLG GEALALKADQ AALLAKADLL TDMVGEFPEL
QGVMGRYYAQ HDGVADDVAF AIEDHYRPRF AGDDLPRNPV GVCVALADKL ETLVGLFGIG
EKPTGDKDPF ALRRHALGVV RMLIEKHLPI GLNELVSIAF SAFQQGLLGQ AHTDVYLFMF
ERLSGAMREQ GYSANEVDAV LSLNPIRIDL VPQQLEAVRA FAALPEAAAL AAANKRVGNI
LKKAEGEVGA SADPGRFVEA AERALFAALD EVAPRAAAAF GSGDYTASLQ ALAALKAPVD
AFFDQVMVNA DDPALRANRL ALLNQLHRTM NRVADISRLA A