ID A0A136L2I9_9BACT Unreviewed; 480 AA.
AC A0A136L2I9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
GN Name=glyS_1 {ECO:0000313|EMBL:KXK15928.1};
GN ORFNames=UZ18_ATM001001451 {ECO:0000313|EMBL:KXK15928.1};
OS Armatimonadetes bacterium OLB18.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK15928.1, ECO:0000313|Proteomes:UP000070351};
RN [1] {ECO:0000313|EMBL:KXK15928.1, ECO:0000313|Proteomes:UP000070351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB18 {ECO:0000313|EMBL:KXK15928.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) 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 -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK15928.1}.
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DR EMBL; JZQX01000137; KXK15928.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136L2I9; -.
DR STRING; 1617424.UZ18_ATM001001451; -.
DR PATRIC; fig|1617424.3.peg.1548; -.
DR Proteomes; UP000070351; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KXK15928.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
SQ SEQUENCE 480 AA; 52324 MW; F33FD50C15CDA7AC CRC64;
MPELFVELGC EELPPSFVRK AASDLSQQIQ QRLEAERIGF IAGSGPFGTP RRLIVHLADV
DAQQPDLKKR VRGPSEAAAF GPEGSPLPAL QGFCRSAGVD PSEVEVEGGY VWAAKVEPGK
PTLEVLRELL PAAIRSLSFE KSTRWSTGRL KFARPIRWVV AVLGGANRRI RTRVRALRPR
EPGPQVLGER VVRGRKLRRS DVGFEGAFVE PDPAQRERMI REGSLDASSG MAELTDALVD
ENVMLTEWPM PTLGGFDEGY LALPEPVLIT AMAKHERMFP VRSPGGELLP QFVFVRNSGE
ESVVSEGARW VLSARFNDAK FFFEEDRART LEEFRETTAG ILLHEKLGSI LDRSNRIGKL
AEFLARTNGQ SDEVVGAAAE AGRLCKADLS TGLVSELASL QGIVGGIYAR RDGLPEAVAA
GIEGHYDLGR ALEAAVKGEP VALLVLIADQ LDKLFGYLVG GSLRLRGRRT LTVFAARQAN
//
