GLUQ_PROMM
ID GLUQ_PROMM Reviewed; 306 AA.
AC Q7TUT1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glutamyl-Q tRNA(Asp) synthetase {ECO:0000255|HAMAP-Rule:MF_01428};
DE Short=Glu-Q-RSs {ECO:0000255|HAMAP-Rule:MF_01428};
DE EC=6.1.1.- {ECO:0000255|HAMAP-Rule:MF_01428};
GN Name=gluQ {ECO:0000255|HAMAP-Rule:MF_01428}; OrderedLocusNames=PMT_1394;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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:0000255|HAMAP-Rule:MF_01428}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01428};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01428};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC GluQ subfamily. {ECO:0000255|HAMAP-Rule:MF_01428}.
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DR EMBL; BX548175; CAE21569.1; -; Genomic_DNA.
DR RefSeq; WP_011130762.1; NC_005071.1.
DR AlphaFoldDB; Q7TUT1; -.
DR SMR; Q7TUT1; -.
DR STRING; 74547.PMT_1394; -.
DR EnsemblBacteria; CAE21569; CAE21569; PMT_1394.
DR KEGG; pmt:PMT_1394; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_0_0_3; -.
DR OMA; WLLRMED; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000001423; Chromosome.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; -; 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 Pfam; PF00749; tRNA-synt_1c; 2.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..306
FT /note="Glutamyl-Q tRNA(Asp) synthetase"
FT /id="PRO_0000208312"
FT MOTIF 32..42
FT /note="'HIGH' region"
FT MOTIF 244..248
FT /note="'KMSKS' region"
FT BINDING 29..33
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 65
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 188
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 206
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01428"
SQ SEQUENCE 306 AA; 34097 MW; 474CFA6E2DA1BE10 CRC64;
MAKSSALPDH LYEQMEVGQR LRNQGYRGRF APSPTGPLHL GNLCTALVSW LQARLANGAW
LLRVDDLDQP RNRVGAVESL QQDLHWLGLE WDGPVVFQSR RRGIYNSFLS ALRRQGKLYA
CRCSRRMLAD ISAPAGRHLV YPGTCRDLEL FWGWHEGRLP SWRLRVSKEF SHTSGDVILR
RADGFIAYHL ATVVDELTLG ISEVVRGEDL LDAMNAQLAL INAISERPVI YRHVPLLCDD
QGRKLAKREG HAGLDSLRSE GLGPSHVVGW LAASQSLVPF GAELTAGELL SELKKKEGVL
KSVLKP
