ID SYGB_GEOMG Reviewed; 686 AA.
AC Q39RG5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=Gmet_2941;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) 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; CP000148; ABB33159.1; -; Genomic_DNA.
DR RefSeq; WP_004512877.1; NC_007517.1.
DR AlphaFoldDB; Q39RG5; -.
DR SMR; Q39RG5; -.
DR STRING; 269799.Gmet_2941; -.
DR KEGG; gme:Gmet_2941; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_7; -.
DR Proteomes; UP000007073; 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 NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 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..686
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006361"
SQ SEQUENCE 686 AA; 74759 MW; 80F12E8A87A3CF78 CRC64;
MKELFLEIGT EEIPAGFIPK AMADMEALLA KELENARISF DDIRTLGTPR RLALTVKGLP
TVQPDAEITA MGPARNVAFD AEGKPTRAAE GFARGQGVDV ASLTLVATEK GEYVAAVRKE
SGRPVPELLA EILPRLVANI PFRKSMRWGA LDVRFARPIH WIVALFDGVV VPFTFGNIES
GTISRGHRFM ANQPFPVRDF AHYLEECERH FVIPDPERRQ EIIRREIHRV AKAAGGHLLP
DEGLLEEVSF LCEYPSAVHG TFSAEFLKVP REVLITSMRS HQRYFSIVDD AGKLMPGFIT
INNTLTEDPT VVVKGNERVL RARLSDARFF FEEDQKVKLE TRVESLKNVV YQQKLGTSFE
KMERFRALAE GLADLLNPAV KVKVSQAAFL CKADLVSGMV GEFPEVQGIM GREYALIEGE
DAEVAAAIAE HYLPTQAGGE LPASDIGAFV SMADKLDTIC GCFGVGLIPT GSADPYALRR
SALGIINIIL DKGYRLSLEE QVDKALGLLA AKLTRPAVDV KADVLEFFRG RFVNLMADRH
ASDAVDAAVA AGCADLVDAA ARIAALSEFR SHPDFEPLAV AFKRVGNIVK EGVDAPVDTA
LFQDAAEGLL NDAVQGVAVS VREKIATGAY LEALTEIAAL RGPVDTFFDK VMVMAEDERV
RTNRLALLTG IARMLGAIAD FAKIAA
//
