ID A0A0X3AQF1_9FLAO Unreviewed; 512 AA.
AC A0A0X3AQF1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=Ga0061079_10532 {ECO:0000313|EMBL:CVK16078.1};
OS Apibacter mensalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Apibacter.
OX NCBI_TaxID=1586267 {ECO:0000313|EMBL:CVK16078.1, ECO:0000313|Proteomes:UP000182761};
RN [1] {ECO:0000313|EMBL:CVK16078.1, ECO:0000313|Proteomes:UP000182761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-53146 {ECO:0000313|EMBL:CVK16078.1,
RC ECO:0000313|Proteomes:UP000182761};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) 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; FCOR01000005; CVK16078.1; -; Genomic_DNA.
DR RefSeq; WP_055425291.1; NZ_LIVM01000005.1.
DR AlphaFoldDB; A0A0X3AQF1; -.
DR STRING; 1586267.GCA_001418685_00917; -.
DR OrthoDB; 9760853at2; -.
DR Proteomes; UP000182761; Unassembled WGS sequence.
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 CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 1.
DR Gene3D; 3.30.40.230; -; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {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:UP000182761}.
FT DOMAIN 176..410
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 152..179
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 249..251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 259..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 264..268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 331..332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 371..375
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
FT BINDING 375..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253"
SQ SEQUENCE 512 AA; 59266 MW; E434154FEB583E83 CRC64;
MKSQEDVLKK VVSHAKEYGF VFPSSEVYDG LSAIYDYGQN GVELKNNIKQ YWWKAMVQLN
ENILGLDSAI FMHPTIWKAS GHIDAFNDPL IDNKDSKKRF RADVLVEEFA EKFEDKAKKE
IEKAKKRFGE AFNLEQFEAT NPKVLECRKQ KADILQRLAK SLETNLADTK ALIEELEISD
PETGSKNWTE VRQFNLMFGT KLGSTADSAT DLYLRPETAQ GIFVNYLNVQ KTGRKKLPFG
IAQIGKAFRN EIVARQFIFR MREFEQMEMQ FFVPPGTELS YFKEWKEKRL NWHLALGLGK
DNYRFHDHEK LAHYANAATD IEFKFPFGFK ELEGIHSRTN FDLSAHEKYS GKKLQYFDPE
QNKSYVPYVV ETSIGLDRMF LALLSKCLKE ETLDDGSSRV VLNLPPALAP NKVAIFPLVK
KDGLPEYAEK IFNDLKFDYN IMYEDKDAIG KRYRRQDAIG TPYCITIDHD TLTNHTVTIR
NRDTMKQERI SVDSLREIIG ENIELKSLLK KI
//
