SYGB_PSEPK
ID SYGB_PSEPK Reviewed; 684 AA.
AC Q88RR9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PP_0060;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN65694.1; -; Genomic_DNA.
DR RefSeq; NP_742230.1; NC_002947.4.
DR RefSeq; WP_010951468.1; NC_002947.4.
DR AlphaFoldDB; Q88RR9; -.
DR SMR; Q88RR9; -.
DR STRING; 160488.PP_0060; -.
DR PRIDE; Q88RR9; -.
DR EnsemblBacteria; AAN65694; AAN65694; PP_0060.
DR KEGG; ppu:PP_0060; -.
DR PATRIC; fig|160488.4.peg.65; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR PhylomeDB; Q88RR9; -.
DR BioCyc; PPUT160488:G1G01-63-MON; -.
DR Proteomes; UP000000556; 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..684
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072919"
SQ SEQUENCE 684 AA; 75113 MW; C6E5561B2794C599 CRC64;
MSAQDFLVEL GTEELPPKAL ASLGDAFLAG IEKGLQAAGL NYTGKQVYAA PRRLAVLIRQ
LDVQQPDRSI NIDGPPLQAA FNAEGEPTQA ALGFAKKCGV ELAEIDQSGP KLRFSQHIPG
KATVGLLPTI VEDSLNDLPI PKRMRWAASR EEFVRPTQWL VMLLGDQVVD CTILSQKAGR
ESRGHRFHHP ENVLITTPAN YVEDLRKAYV LADFAERREL ISKRTAELAM QQEGTAIVPP
ALLDEVTALV EWPVPLVCSF EERFLEVPQE ALITTMQDNQ KYFCLLDSEG KLLPRFITVA
NVESRDPKQI VQGNEKVVRP RLTDAEFFFK QDKKQPLETF NERLKNVVFQ AQLGTVYDKA
ERVSRLAAFI APLIGGDAQR AGRAGLLSKC DLATEMVGEF PEMQGVAGYY YALNDGEPED
VALALNEQYM PRGAGAELPQ TLTGAAVAIA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
GVLRILIEKQ LDLDLTGAVE FAVKQFGAKI KAPGLAEQVL EFIFDRLRAR YEDEGIDVAT
YLSVRALQPG SALDFDQRVQ AVQAFRKLPE AEALAAVNKR VSNLLSKAEG AIAEQVEPKY
FDNANEFSLY SAIQQADQAV QPMAAARQYS ESLARLAALR DPVDAFFEAV MVNAEDAKVR
ANRYALLSRL RGLFLGVADI SLLG