SYGB_ACIF2
ID SYGB_ACIF2 Reviewed; 694 AA.
AC B7J7P8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; OrderedLocusNames=AFE_2581;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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:0000255|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; CP001219; ACK79291.1; -; Genomic_DNA.
DR RefSeq; WP_012537273.1; NC_011761.1.
DR AlphaFoldDB; B7J7P8; -.
DR SMR; B7J7P8; -.
DR STRING; 243159.AFE_2581; -.
DR PaxDb; B7J7P8; -.
DR EnsemblBacteria; ACK79291; ACK79291; AFE_2581.
DR GeneID; 66433541; -.
DR KEGG; afr:AFE_2581; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001362; 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 HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR TIGRFAMs; TIGR00211; glyS; 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..694
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197162"
SQ SEQUENCE 694 AA; 76429 MW; 6657A849EB47712D CRC64;
MSAPEDLLLE LGCEELPARE QMPLQDAATG IIGQLLDAAG LQFGSIHGYV TPRRLALWIK
DVSRQSLPQE TLRRGPLVAR ARDAQGKPTA AAEGFARSCG VSLDDLLTLE TEKGPVLAWR
EVGTAQDSHA LLPEIASRLV TSLPLRKRMR WGAGSDSFLR PVRWLLLRQG GQVLDWKMFG
LDAGGESFGH RVHHPQAVRI STPAGYAGSL LQAKVMVDFA ERRAHISGKM AALADEMAVT
PILPEALLDE ITGLNEWPVV LAGSFAADYL RVPEEALITV MMQHQRYVPL RGRNERLVPH
YLFAANLHSR DTQVVIDGNN RVLRARLADA AFFWDQDRQI SLQTRRAALA GVLFQDGLGS
ILDKTVRLQE LAAALSPQFA VDAGDMNRAA ALCKSDLLSG LVGEFPELQG IMGGHYARHD
GENNRVATAI AQHYLPSGRD DEIPADAHGQ CLAIADKLDT LCGFFAIGKV PTGDRDPFAL
RRAALGVLRI VLDAGVPLNL DEAVTRTLAA YGGAFARNRT EIRSAILDFF QDRMRVYFRE
EGFRADQIAA VLSRQPHEPL DARQRLEALA LFQAEHAAAD ALAALIKRIN NLLRKEVISG
DWPIDPQYFM DPVENTLWDY WQALEQPLHA QLAERRYTAA LGLLAGLRPA VDQFFDGVMV
LAEDPVLRQN RLALLARLQE AFLRIADFSQ LQGA