ID E6X1V6_NITSE Unreviewed; 297 AA.
AC E6X1V6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254};
GN OrderedLocusNames=Nitsa_0697 {ECO:0000313|EMBL:ADV45964.1};
OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Nitratifractor.
OX NCBI_TaxID=749222 {ECO:0000313|EMBL:ADV45964.1, ECO:0000313|Proteomes:UP000008633};
RN [1] {ECO:0000313|EMBL:ADV45964.1, ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RX PubMed=21886859;
RA Anderson I., Sikorski J., Zeytun A., Nolan M., Lapidus A., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Ngatchou-Djao O.D., Rohde M., Tindall B.J., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Nitratifractor salsuginis type strain (E9I37-
RT 1).";
RL Stand. Genomic Sci. 4:322-330(2011).
RN [2] {ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nitratifractor salsuginis DSM 16511.";
RL Submitted (JAN-2011) 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:0000256|ARBA:ARBA00000201,
CC ECO:0000256|HAMAP-Rule:MF_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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DR EMBL; CP002452; ADV45964.1; -; Genomic_DNA.
DR RefSeq; WP_013553658.1; NC_014935.1.
DR AlphaFoldDB; E6X1V6; -.
DR STRING; 749222.Nitsa_0697; -.
DR KEGG; nsa:Nitsa_0697; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_7; -.
DR OrthoDB; 9802183at2; -.
DR Proteomes; UP000008633; 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 CDD; cd00733; GlyRS_alpha_core; 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 NCBIfam; TIGR00388; glyQ; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00254};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00254};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00254}; Reference proteome {ECO:0000313|Proteomes:UP000008633}.
SQ SEQUENCE 297 AA; 33986 MW; BDD53F86C70E5B35 CRC64;
MNPNAITFSD LLLKLQQYWA AQGCTIVQPY DLPAGAGTFH PATLLRSLDS TPWATAYVAP
SRRPTDGRYG ENPNRLGAYY QFQVLIKPSP DNIQDLYLKS LEYLGLRLQD HDIRFVEDNW
ESPTLGAWGL GWEVWLDGME VTQFTYFQQV GGLPCDPVAV EITYGTERLA MYLQGVESVF
DIVWNRKGDE VVTYADVHKE SEYEFSKYHF EVADTEMLFR HFDDASNECR RCLEAGLPLP
AYDQCMIASH TFNVLDARKA ISQAQRQNYI LKIRDLAKGC AELYKAQEPE RLKRVKS
//