ID A0A0A1H0N5_9BURK Unreviewed; 311 AA.
AC A0A0A1H0N5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000256|HAMAP-Rule:MF_01428};
DE Short=Glu-Q-RSs {ECO:0000256|HAMAP-Rule:MF_01428};
DE EC=6.1.1.- {ECO:0000256|HAMAP-Rule:MF_01428};
GN Name=gluQ {ECO:0000256|HAMAP-Rule:MF_01428};
GN ORFNames=E1O_07420 {ECO:0000313|EMBL:BAP87873.1};
OS Burkholderiales bacterium GJ-E10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1469502 {ECO:0000313|EMBL:BAP87873.1, ECO:0000313|Proteomes:UP000031649};
RN [1] {ECO:0000313|EMBL:BAP87873.1, ECO:0000313|Proteomes:UP000031649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GJ-E10 {ECO:0000313|EMBL:BAP87873.1,
RC ECO:0000313|Proteomes:UP000031649};
RA Fukushima J., Tojo F., Asano R., Kobayashi Y., Shimura Y., Okano K.,
RA Miyata N.;
RT "Complete Genome Sequence of the Unclassified Iron-Oxidizing,
RT Chemolithoautotrophic Burkholderiales bacterium GJ-E10 Isolated from Acid
RT River.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the tRNA-independent activation of glutamate in
CC presence of ATP and the subsequent transfer of glutamate onto a
CC tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-
CC cyclopenten-1-yl) moiety of the queuosine in the wobble position of the
CC QUC anticodon. {ECO:0000256|HAMAP-Rule:MF_01428}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01428};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01428};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC GluQ subfamily. {ECO:0000256|HAMAP-Rule:MF_01428}.
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DR EMBL; AP014683; BAP87873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1H0N5; -.
DR STRING; 1469502.E1O_07420; -.
DR KEGG; bbag:E1O_07420; -.
DR HOGENOM; CLU_015768_0_1_4; -.
DR Proteomes; UP000031649; Chromosome.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01428; Glu_Q_tRNA_synth; 1.
DR InterPro; IPR022380; Glu-Q_tRNA(Asp)_Synthase.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR03838; queuosine_YadB; 1.
DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR PANTHER; PTHR43311:SF1; GLUTAMYL-Q TRNA(ASP) SYNTHETASE; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_01428};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01428};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01428};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01428};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01428}; Protein biosynthesis {ECO:0000256|RuleBase:RU363037};
KW Reference proteome {ECO:0000313|Proteomes:UP000031649};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01428}.
FT DOMAIN 22..265
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT MOTIF 25..35
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT MOTIF 259..263
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 22..26
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 58
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 203
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 221
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
SQ SEQUENCE 311 AA; 33266 MW; F20C17292A6F40AD CRC64;
MVPGTLADPS APMAAPAAYV GRFAPSPTGP LHRGSLAAAL ASWLDARAHG GQWLVRIEDV
DGPRCRPGAE ETILAQLAAC GLHPDRPVIR QRDRTAAYRR ALYALRTDGL AYPCACSRRA
IEEALVQQGM APERHAERIY PGTCRAGIAE GAPDGPRAWR LRVPEGTAAH VDWVDRRLGP
HSEAVDRTVG DFVLLRADGM WAYQLAVVVD DAGQGVTDVV RGEDLADSTA RQVLLQRMLG
LATPRYLHVP LVRDEAGEKL SKQTGAAAFV PGPAALVQAM RDLGLGSSDA TTVPDLLTAA
TDRWRALWGE A
//
