SYGB_PSEP1
ID SYGB_PSEP1 Reviewed; 684 AA.
AC A5VWJ1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Pput_0076;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000712; ABQ76251.1; -; Genomic_DNA.
DR RefSeq; WP_011953119.1; NC_009512.1.
DR AlphaFoldDB; A5VWJ1; -.
DR SMR; A5VWJ1; -.
DR STRING; 351746.Pput_0076; -.
DR EnsemblBacteria; ABQ76251; ABQ76251; Pput_0076.
DR KEGG; ppf:Pput_0076; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
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..684
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006392"
SQ SEQUENCE 684 AA; 75108 MW; 4C2B9CCD647658B6 CRC64;
MSAQDFLVEL GTEELPPKAL TSLGEAFLAG IEKGLQAAGL NYTGKQVYAA PRRLAVLIRQ
LDVQQPDRSI NIDGPPLQAA FNAEGEPTQA ALGFAKKCGV ELAEIDQSGP KLRFSQHIPG
KATTDLLPTI VEDSLNDLPI PKRMRWAASR EEFVRPTQWL VMLLGDQVVD CTILSQKAGR
ESRGHRFHHP ETVVITTPAN YVEDLRKAHV LADFAERREL ISKRTAELAM QQEGTAIVPP
ALLDEVTALV EWPVPLVCSF EERFLEVPQE ALITTMQDNQ KYFCLLDSEG KLLPRFITVA
NIESRDPKQI VQGNEKVVRP RLTDAEFFFK QDKKQPLETF NERLKNVVFQ AQLGTVYDKA
ERVSKLAAFV APLIGGDAQR AGRAGLLSKC DLATEMVGEF PEMQGVAGYY YALNDGEPED
VALALNEQYM PRGAGAELPQ TLTGAAVAIA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
GVLRILIEKQ LDLDLTGAVE FAVKQFGAKV KAPGLADQVL EFIFDRLRAR YEDEGIDVAT
YLSVRALQPG SALDFDQRVQ AVQAFRKLPE AEALAAVNKR VSNLLSKAEG AIAEQVEPKY
FDNANEFSLY SAIQQADQAV QPMAAARQYS ESLARLAALR DPVDAFFEAV MVNAEDAKVR
ANRYALLSRL RGLFLGVADI SLLG