ID R4K9L7_CLOPA Unreviewed; 463 AA.
AC R4K9L7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Glycine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00253};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00253};
DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00253};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00253};
GN Name=glyQS {ECO:0000256|HAMAP-Rule:MF_00253};
GN ORFNames=Clopa_4558 {ECO:0000313|EMBL:AGK99258.1};
OS Clostridium pasteurianum BC1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK99258.1, ECO:0000313|Proteomes:UP000013523};
RN [1] {ECO:0000313|EMBL:AGK99258.1, ECO:0000313|Proteomes:UP000013523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1 {ECO:0000313|EMBL:AGK99258.1,
RC ECO:0000313|Proteomes:UP000013523};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00253};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00253}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00253}.
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DR EMBL; CP003261; AGK99258.1; -; Genomic_DNA.
DR RefSeq; WP_015617527.1; NC_021182.1.
DR AlphaFoldDB; R4K9L7; -.
DR STRING; 86416.Clopa_4558; -.
DR KEGG; cpas:Clopa_4558; -.
DR PATRIC; fig|86416.3.peg.4558; -.
DR eggNOG; COG0423; Bacteria.
DR HOGENOM; CLU_015515_2_1_9; -.
DR OrthoDB; 9760853at2; -.
DR Proteomes; UP000013523; 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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00389; glyS_dimeric; 1.
DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00253};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00253};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00253};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00253};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00253};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00253}; Reference proteome {ECO:0000313|Proteomes:UP000013523}.
FT DOMAIN 157..370
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 207..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 217..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 222..226
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 291..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 331..335
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 335..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ SEQUENCE 463 AA; 53558 MW; CF7502C88E4AD8EA CRC64;
MSFEKTMEKI VALAKNRGFI FPGSDIYGGL ANSWDYGPLG VEFKNNVKKA WWKKFIQESP
YNVGLDCAIL MNREVWVASG HVGGFSDPLM DCKDCKSRFR ADKLVEEHMV SKGIDYASAD
GFTNEQLKEY IEKNNIVCPK CGKSNFTDIR KFNLMYKTFQ GVTEDSKSEI FLRPETAQGI
FVNFKNVQRS SRKKIPFGIG QIGKAFRNEI TPGNFIFRIR EFEQMELEFF CKPGTDLEWF
KYWKDYSLNF LLNLGINKDN IRMRDHSPEE LVFYSKATSD IEYKFPFGWG ELWGVADRTD
YDLSKHMEHS GEDLNYLDPT NNEKYIPYVI EPSLGADRVT LAFLVDAYGE EELEGGDVRT
VLHLHPALAP FKAAILPLSK KLSEKSIEVY NKLSKNFNVD YDEAGSIGKR YRREDEIGTP
YCITIDFDTL EDETVTVRDR DTMQQERVKI EELEKFIEDK LNF
//
