ID A0A0U3GNH6_9MICC Unreviewed; 312 AA.
AC A0A0U3GNH6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ECO:0000313|EMBL:GEO90857.1};
GN ORFNames=AS188_14495 {ECO:0000313|EMBL:ALU40755.1}, KFL01_01630
GN {ECO:0000313|EMBL:GEO90857.1};
OS Kocuria flava.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU40755.1, ECO:0000313|Proteomes:UP000057181};
RN [1] {ECO:0000313|EMBL:ALU40755.1, ECO:0000313|Proteomes:UP000057181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO-9041 {ECO:0000313|EMBL:ALU40755.1,
RC ECO:0000313|Proteomes:UP000057181};
RA Zhou M., Dai J.;
RT "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GEO90857.1, ECO:0000313|Proteomes:UP000321155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107626 {ECO:0000313|EMBL:GEO90857.1,
RC ECO:0000313|Proteomes:UP000321155};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kocuria flava NBRC 107626.";
RL Submitted (JUL-2019) 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; CP013254; ALU40755.1; -; Genomic_DNA.
DR EMBL; BJZR01000002; GEO90857.1; -; Genomic_DNA.
DR RefSeq; WP_058859436.1; NZ_CP013254.1.
DR AlphaFoldDB; A0A0U3GNH6; -.
DR STRING; 446860.AS188_14495; -.
DR KEGG; kfv:AS188_14495; -.
DR OrthoDB; 9807503at2; -.
DR Proteomes; UP000057181; Chromosome.
DR Proteomes; UP000321155; Unassembled WGS sequence.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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:UP000057181};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01428}.
FT DOMAIN 15..271
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 18..28
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT MOTIF 242..246
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 15..19
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 51
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 186
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 204
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
SQ SEQUENCE 312 AA; 33460 MW; EE7691C4FB240E09 CRC64;
MTSDGTGDAP RGAGRYAPSP SGDLHVGNLR TALLAWALAR GSGRSFVLRI EDLDRVRPGA
ARRQLADLAR TGLDWDGEPL LQSTREAAHR AVVERLTAAG LTYECYCTRR EIRAAASAPH
GAPGAYPGTC RDLGPAERAV RRAGRAPAVR LRAQVHEETV LDRWAGPYTG AVDDLVLLRN
DGRPAYNLAV VLDDAHQGVD QVVRGDDLLP STPRQAHLAD LLGLPRPEWV HVPLVLNPQG
QRLAKRDGAV TLADLGAAGV PAEEAVARIV ASLGLPGRPR TAQDVLAVLD EDVLPRVPWV
LDPRKWTAQR TG
//
