SYGB_SYNWW
ID SYGB_SYNWW Reviewed; 688 AA.
AC Q0AWT6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=Swol_1515;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68818.1; -; Genomic_DNA.
DR RefSeq; WP_011640917.1; NC_008346.1.
DR AlphaFoldDB; Q0AWT6; -.
DR SMR; Q0AWT6; -.
DR STRING; 335541.Swol_1515; -.
DR EnsemblBacteria; ABI68818; ABI68818; Swol_1515.
DR KEGG; swo:Swol_1515; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001968; 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; Reference proteome.
FT CHAIN 1..688
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101364"
SQ SEQUENCE 688 AA; 78244 MW; 43B5251B5989F3E0 CRC64;
MAQDLLLEIG VEEMPSAYMP RVLKDLKDLA QKNLAEARLS CGEVLTLGTP RRLCLWVKEI
SEEQEDSLLE NRGPKKSIAF DANGNPSKAG LGFARSQGVD FRELQIREVS GVEYLFAIKK
EKGQAAEQIL PGLLLKVIHS LSFPKSMTWS YYQTRFARPI RWLLAIFGDK NVEFNIENIK
SANYTYGHRF LSTGVLLVTS IDDYFRVLRE HYVILDQAER KKMIWQQVQK VAGEAGGKAM
ENEELLEEVA FLVEFPTAFY GEFSPSYLDV PPEVLTTSMI EHQRYFPVYN NEGRLLPGFV
GVRNGTDYCL DIVRAGNERV LKARLEDALF FWNEDSRKSL EEMSAKLKNV LFHERLGTLA
DKVLRLQKLA LFIGQQTGLG QPEKLQRSAL LCKADLMSNM VYEFPELQGI MGRYYASGSA
EEPEVAEAIF EHYLPRFAGD KLPSSAGGIV LSLAEKMDNL MGCFSIGIKP SGSQDPYALR
RQALGLVNII LDKKLSIDLK LVFEQAYLGY KDIDLEKSRE DSVKELLDFI YQRMRGVLLD
NGISYDVVDA ALSRPSFDLF ETYYRAFKLQ EFKKSPVFED FMVVYNRVHN LSRKWESEEI
DLDLLVDESE KNLCQKLPGL QEDIKKSLIA QDYTRALELL AALRADIDQF FTAVMVMVDD
ERLKAARLGI LKSIANMFNS IADFSKIV