ID A0A1H1B2N1_9ACTN Unreviewed; 283 AA.
AC A0A1H1B2N1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=SAMN04489765_0510 {ECO:0000313|EMBL:SDQ46199.1};
OS Tsukamurella pulmonis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=47312 {ECO:0000313|EMBL:SDQ46199.1, ECO:0000313|Proteomes:UP000183053};
RN [1] {ECO:0000313|Proteomes:UP000183053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA Varghese N.;
RL Submitted (OCT-2016) 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; FNLF01000002; SDQ46199.1; -; Genomic_DNA.
DR RefSeq; WP_068564880.1; NZ_UHII01000001.1.
DR AlphaFoldDB; A0A1H1B2N1; -.
DR STRING; 47312.SAMN04489765_0510; -.
DR OrthoDB; 9807503at2; -.
DR Proteomes; UP000183053; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_01428}.
FT DOMAIN 5..239
FT /note="Glutamyl/glutaminyl-tRNA synthetase class Ib
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00749"
FT MOTIF 8..18
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT MOTIF 228..232
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 5..9
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 41
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 112
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 172
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 190
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01428"
SQ SEQUENCE 283 AA; 30609 MW; 165436F322CDCF40 CRC64;
MTAGRYAPSP SGDLHVGNLR TALLAWLFAR STGREFLLRV EDLDRVAGGA EARQLADLAA
IGLDWDGAPV RQSARTDVYA AALTRLDVYE CYCTRREILA APSAPHAPEG AYPGTCRDLT
EAQRVERRRE RPAALRLRAT VDEFTVTDVL HGEYTGAVDD FVLRRGDGTY AYNLAVVVDD
AAQGVDQVVR GDDLLSSAPR QAYLGTLLGD PPPTYAHVPM VLGPNGVRLA KRDGAVTLAD
RGGPGVVLPE IAASLGLRGR TPREMLDDFD PARLPREPWT LPL
//
