ID Q5P765_AROAE Unreviewed; 315 AA.
AC Q5P765;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 ECO:0000313|EMBL:CAI06846.1};
GN ORFNames=ebA1331 {ECO:0000313|EMBL:CAI06846.1};
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06846.1, ECO:0000313|Proteomes:UP000006552};
RN [1] {ECO:0000313|EMBL:CAI06846.1, ECO:0000313|Proteomes:UP000006552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI06846.1,
RC ECO:0000313|Proteomes:UP000006552};
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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|ARBA:ARBA00011209, 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; CR555306; CAI06846.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5P765; -.
DR STRING; 76114.ebA1331; -.
DR KEGG; eba:ebA1331; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_4; -.
DR Proteomes; UP000006552; 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:UP000006552}.
SQ SEQUENCE 315 AA; 35636 MW; D29A2BB2C82CF1F9 CRC64;
MPPLQPSETM SPHKPTFQQV ILTLQQYWGE RGCVLLQPYD LEVGAGTSHT ATFLRAIGPE
PWNAAYVQPS RRPKDGRYGE NPNRLQHYYQ FQVVLKPSPL NIQELYLDSL RALGIDTNAH
DIRFVEDDWE NPTLGAWGLG WEVWLDGMEV TQFTYFQQVG GLDCKPVLGE ITYGLERLAM
YLQGVENVYD LVWAVYPDGS KVTYGDVFHQ NEVEQSTYNF EHSNVDFFFS LFGNYEAEAK
RLMEAGLALP AYEMVLKAAH SFNMLDARGA ISVTERAAYI GRIRNLSRAV AQAYSASRES
LGFPMLNQNP SQEAA
//