SYGB_LIMF3
ID SYGB_LIMF3 Reviewed; 692 AA.
AC B2GBZ7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=LAF_0843;
OS Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS fermentum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=334390;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3956 / LMG 18251;
RX PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA Hattori M.;
RT "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT fermentum reveal a genomic island for reuterin and cobalamin production.";
RL DNA Res. 15:151-161(2008).
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; AP008937; BAG27179.1; -; Genomic_DNA.
DR RefSeq; WP_012391176.1; NC_010610.1.
DR AlphaFoldDB; B2GBZ7; -.
DR SMR; B2GBZ7; -.
DR EnsemblBacteria; BAG27179; BAG27179; LAF_0843.
DR GeneID; 61200414; -.
DR KEGG; lfe:LAF_0843; -.
DR PATRIC; fig|334390.5.peg.927; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001697; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 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..692
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101292"
SQ SEQUENCE 692 AA; 77403 MW; C819B1338817199B CRC64;
MAHSYLLEVG LEEMPAHVVT PSIQQLKTRV ANYLTEERID FEDIQAYSTP RRLALLISGL
ADKQPDVDES VKGPAKKIAQ DADGNWTKAA IGFTRGQGAT VDDIEFKEVK GVEYVYVEKH
IQGKPVAEVL AGLNDVITAM NFPTLMRWGS FKLNFIRPIH WLVSLLDDQV VPFDILNVTA
GRLTRGHRFL GHDVEIKSAT DYVAALKDDF VIVDAAERKA TIKDQIQAIV DQHNWVIDWD
EELLEEVNNL VEWPTAFAGT FDQKYLELPE PVLITSMKDN QRFFCVRDHD GKLQPAFISV
RNGNAVHLDN VIKGNERVLV PRLEDAKFFF DEDQKMTIDQ YVDRLKNVSF HDQISSMYDK
MARTKALANL LGQQLGLSDQ ELADLARAAS IYKFDLTTQM VGEFAELQGI MGEIYAKRFG
ENEAVAAAVR EHYMPISADG ALPQTTVGTV LAIADKLDSI YSFFAVDMIP SGSNDPYALR
RQAYGIVRML ADRKWHLNLL DFQASAKQAV EQATPALGLD YAKNADAVTD FFIDRLKQLF
SLDHLRHDIV DAVTDTHVTD PAAIVEAAHV LDAHKDDADL KDQVEALTRV IRLAAKGNLS
EDDVKVDPSL FENPSEGQLD QAVQALIDAK EGRSLDQQFS ALLELEPVIS LYFEENMIMD
KDEAVKNNRL SLLTILADQT AAFGNLDQLI VK