ID SYG_BIFLO Reviewed; 490 AA.
AC Q8G7W9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 66.
DE RecName: Full=Glycine--tRNA ligase;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase;
DE Short=GlyRS;
GN Name=glyQS; Synonyms=glyS; OrderedLocusNames=BL0116;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B.,
RA Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M.,
RA Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation
RT to the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly) (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC + glycyl-tRNA(Gly).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
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DR EMBL; AE014295; AAN23981.1; -; Genomic_DNA.
DR RefSeq; NP_695345.1; NC_004307.2.
DR ProteinModelPortal; Q8G7W9; -.
DR STRING; 206672.BL0116; -.
DR EnsemblBacteria; AAN23981; AAN23981; BL0116.
DR GeneID; 1023037; -.
DR KEGG; blo:BL0116; -.
DR PATRIC; 21117279; VBIBifLon107831_0125.
DR eggNOG; COG0423; -.
DR HOGENOM; HOG000242016; -.
DR KO; K01880; -.
DR OMA; DLSYFDQ; -.
DR ProtClustDB; PRK04173; -.
DR BioCyc; BLON206672:GI1E-116-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1; -.
DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR022961; Gly_tRNA_ligase_bac.
DR InterPro; IPR002315; tRNA-synt_gly.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF52954; Anticodon_bd; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1 490 Glycine--tRNA ligase.
FT /FTId=PRO_0000072948.
FT NP_BIND 195 197 ATP (By similarity).
FT NP_BIND 205 210 ATP (By similarity).
FT NP_BIND 282 283 ATP (By similarity).
FT NP_BIND 326 329 ATP (By similarity).
FT REGION 210 214 Substrate binding (By similarity).
FT REGION 322 326 Substrate binding (By similarity).
FT BINDING 99 99 Substrate (By similarity).
FT BINDING 163 163 Substrate (By similarity).
SQ SEQUENCE 490 AA; 55909 MW; 05C0226128BF09D2 CRC64;
MAQSKLDEVV SLAKRRGFVF PAGEIYGGTR SAWDYGPLGV ALKDNIKREW WRSMVVTRPD
VVGVDTSIIL PPEVWVASGH VSVFNDPLVE CLNCHKRNRA DKLEESYAEK HGDKMPENGM
KDIVCPNCGI RGQWTEPRDF NMMLRTHLGP VEDENSLHYL RPETAQGIFV DFKNVMTSSR
SRPPFGIANM GKSFRNEITP GNFIFRTREF EQMEMEFFVT PGTDEEWHQY WIDARTRWYI
DLGVKPENLR HYEHPKEKLS HYSKRTVDIE YKFGFQGSDW GELEGIANRT DYDLSAHSKH
SGEDLSYFNQ ATGEKYVPYV IEPAAGLTRS LMCFLVDAYD VDEAPNTKGG VDKRTVLRLD
PRLAPVKAAV LPLSKKPELQ TVAQNLADDL RFNEWMIDYD ESGAIGRRYR RQDEIGTPLC
ITVDFDTLED HAVTIRERDT MAQERVALDK VADYVAARIG EKRTRVPLKP VEMGGEPWPE
SGVQEAGGLY
//
