SYGA_VIBCH
ID SYGA_VIBCH Reviewed; 305 AA.
AC Q9KVW7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Glycine--tRNA ligase alpha subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE Short=GlyRS;
GN Name=glyQ; OrderedLocusNames=VC_0021;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF93199.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93199.1; ALT_INIT; Genomic_DNA.
DR PIR; G82373; G82373.
DR RefSeq; NP_229680.2; NC_002505.1.
DR RefSeq; WP_001174901.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KVW7; -.
DR SMR; Q9KVW7; -.
DR STRING; 243277.VC_0021; -.
DR DNASU; 2614961; -.
DR EnsemblBacteria; AAF93199; AAF93199; VC_0021.
DR GeneID; 57991274; -.
DR GeneID; 66938336; -.
DR KEGG; vch:VC_0021; -.
DR PATRIC; fig|243277.26.peg.20; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_6; -.
DR OMA; SYYQFQV; -.
DR Proteomes; UP000000584; Chromosome 1.
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; cd00733; GlyRS_alpha_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00388; glyQ; 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..305
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_0000072878"
SQ SEQUENCE 305 AA; 35038 MW; 23AA9D1E5DEC742E CRC64;
MQKYDIKTFQ GMILALQDYW AQQGCTIVQP LDMEVGAGTS HPMTCLRALG PEPIATAYVQ
PSRRPTDGRY GENPNRLQHY YQFQVIIKPS PDNIQELYLG SLRVLGVDPC VHDIRFVEDN
WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGIERL AMYIQGVDSV
YDLVWTDGPL GKVTYGDIFH QNEVEQSTYN FEHADVDFLF TYFDQCEKEC KYLLELEKPL
PLPAYERILK AAHAFNLLDA RKAISVTERQ RYILRIRNLT KSVAEAYYAS REALGFPMCK
KSEQK