SYG_ALKMQ
ID SYG_ALKMQ Reviewed; 462 AA.
AC A6TSJ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253};
GN Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; OrderedLocusNames=Amet_3022;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., 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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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_00253};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00253}.
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DR EMBL; CP000724; ABR49162.1; -; Genomic_DNA.
DR RefSeq; WP_012064129.1; NC_009633.1.
DR AlphaFoldDB; A6TSJ4; -.
DR SMR; A6TSJ4; -.
DR STRING; 293826.Amet_3022; -.
DR EnsemblBacteria; ABR49162; ABR49162; Amet_3022.
DR KEGG; amt:Amet_3022; -.
DR eggNOG; COG0423; Bacteria.
DR HOGENOM; CLU_015515_2_1_9; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 626850at2; -.
DR Proteomes; UP000001572; 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; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR PANTHER; PTHR10745; PTHR10745; 3.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..462
FT /note="Glycine--tRNA ligase"
FT /id="PRO_1000125525"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 216..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 221..225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 290..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 330..334
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
FT BINDING 334..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00253"
SQ SEQUENCE 462 AA; 53478 MW; 9919A9FF363D92B7 CRC64;
MTTAKSMEKI VALAKSRGFI FPGSEIYGGL ANTWDYGPLG VELKNNVKKA WWKKFIQQSP
YNVGLDSAIL MNPTTWEASG HIGGFSDPLM DCKKCRARFR ADKLIEDHFA KDGEDTIVDG
WSNEQMASFI DEKAIVCPEC DAKEFTDIRQ FNLMFKTHQG VNEDTSTEIF LRPETAQGIF
VNFKNVQRTA RKKIPFGIGQ IGKSFRNEIT PGNYTFRTRE FEQMELEFFC KPGDDLEWFD
YWSNFCKKWL LDLSMKETSI RLRAHTEEEL SHYSNATTDI EFKFPFGWGE LWGIADRTDF
DLKQHTEHSG VQLIYQDPVT NEKYVPYCIE PSLGADRVTL AFLVDAYEEE QIDEKDSRIV
LKLHPALAPF KAAVLPLTKK LKEQSLELFE KLSDKFMIDY DDAGSIGKRY RRHDEIGTPY
CITYDFDTLE DNCVTVRDRD TMEQQRVAID ELEVFLEEKI KF
