SYGB_DECAR
ID SYGB_DECAR Reviewed; 712 AA.
AC Q47A67;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-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=Daro_3535;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(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_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; CP000089; AAZ48264.1; -; Genomic_DNA.
DR RefSeq; WP_011289260.1; NC_007298.1.
DR AlphaFoldDB; Q47A67; -.
DR SMR; Q47A67; -.
DR STRING; 159087.Daro_3535; -.
DR EnsemblBacteria; AAZ48264; AAZ48264; Daro_3535.
DR KEGG; dar:Daro_3535; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_4; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
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.
FT CHAIN 1..712
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101269"
SQ SEQUENCE 712 AA; 75036 MW; 5F0FA74B7E901238 CRC64;
MSSKNLLVEL FVEELPPKAL KKLGEAFSAA LANSLKNAGL APATASITAY ASPRRLAAHV
TDVAAVAADK PVAQKLMPVA VGLDAAGNAT PALLKKLAGL GIDADAAASV VASLRRENDG
KADVLFFDSL AKGATLAEGL QKAIEAALAA LPIPKVMTYQ LQDGWSSVNF VRPAHGLVAL
HGGDVVPVAV LGLNAGRETH GHRFEATVDP VVFANADEYA SKLATDGAVI ASFAERRAEI
ARQLEGAAAK AGQATGAALR PIDDEALLDE VTALVERPNV LIGQFEQEFL AVPQECLILT
MKANQKYFPL LDATGKLTNK FLVVSNISPE DASAVIGGNE RVVRPRLADA KFFFDQDRKK
SLESRVIGLS KVVYHNKLGT QGERMQRVAA IARAIGESLG GEALALHAEQ AAVLAKADLL
TDMVGEFPEL QGTMGRYYAL HDGLAAEIAD AVEDHYKPRF AGDTLPRGIV GTVVALADKL
ETLVGMFGIG QIPTGDRDPF ALRRHALGVI RMLAENNLAL PLDHLLQTAA APFASVDGFK
AAEAPLADFI YDRLAGSLRE QGYTAQEVDA VVSQRPQRLG DIPKRLAAVR AFSGLPESAA
LAAANKRVGN ILKKVENAVE AVVDNALLKE AAEIALHDAL VEVVPQADAA FVTGDYSESL
QALAALRAPV DAFFDDVMVN AEDPALRANR LGLLAKLHAA MNQVADISKL SA