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Queuine tRNA-ribosyltransferase (EC 2.4.2.29) (Guanine insertion enzyme) (tRNA-guanine transglycosylase)

 R0EH98_CAUVI            Unreviewed;       371 AA.
R0EH98;
26-JUN-2013, integrated into UniProtKB/TrEMBL.
26-JUN-2013, sequence version 1.
28-MAR-2018, entry version 37.
RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00102053};
EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00384033};
AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_00168};
AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_00168};
Name=tgt {ECO:0000256|HAMAP-Rule:MF_00168};
ORFNames=OR37_02685 {ECO:0000313|EMBL:ENZ81419.1};
Caulobacter vibrioides OR37.
Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
Caulobacteraceae; Caulobacter.
NCBI_TaxID=1292034 {ECO:0000313|EMBL:ENZ81419.1, ECO:0000313|Proteomes:UP000013063};
[1] {ECO:0000313|EMBL:ENZ81419.1, ECO:0000313|Proteomes:UP000013063}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR37 {ECO:0000313|EMBL:ENZ81419.1,
ECO:0000313|Proteomes:UP000013063};
PubMed=23792749;
Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M.,
Epstein S.E., Palumbo A.V., Brown S.D.;
"Draft Genome Sequence for Caulobacter sp. Strain OR37, a Bacterium
Tolerant to Heavy Metals.";
Genome Announc. 1:0-0(2013).
-!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue
with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at
position 34 (anticodon wobble position) in tRNAs with GU(N)
anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs
through a double-displacement mechanism. The nucleophile active
site attacks the C1' of nucleotide 34 to detach the guanine base
from the RNA, forming a covalent enzyme-RNA intermediate. The
proton acceptor active site deprotonates the incoming PreQ1,
allowing a nucleophilic attack on the C1' of the ribose to form
the product. After dissociation, two additional enzymatic
reactions on the tRNA convert PreQ1 to queuine (Q), resulting in
the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
{ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
ECO:0000256|SAAS:SAAS00628203}.
-!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7-
carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.
{ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
ECO:0000256|SAAS:SAAS00102009}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|RuleBase:RU003777};
Note=Binds 1 zinc ion per subunit.
{ECO:0000256|RuleBase:RU003777};
-!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00384008}.
-!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible
for RNA recognition and catalysis, while the other monomer binds
to the replacement base PreQ1. {ECO:0000256|SAAS:SAAS00628204}.
-!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
{ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
ECO:0000256|SAAS:SAAS01002254}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00168}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ENZ81419.1}.
-----------------------------------------------------------------------
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EMBL; APMP01000017; ENZ81419.1; -; Genomic_DNA.
RefSeq; WP_004620671.1; NZ_APMP01000017.1.
EnsemblBacteria; ENZ81419; ENZ81419; OR37_02685.
PATRIC; fig|1292034.3.peg.2660; -.
OrthoDB; POG091H00XO; -.
UniPathway; UPA00392; -.
Proteomes; UP000013063; Unassembled WGS sequence.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
Gene3D; 3.20.20.105; -; 1.
HAMAP; MF_00168; Q_tRNA_Tgt; 1.
InterPro; IPR004803; TGT.
InterPro; IPR036511; TGT-like_sf.
InterPro; IPR002616; tRNA_ribo_trans-like.
Pfam; PF01702; TGT; 1.
SUPFAM; SSF51713; SSF51713; 1.
TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
TIGRFAMs; TIGR00449; tgt_general; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000013063};
Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS01002259,
ECO:0000313|EMBL:ENZ81419.1};
Metal-binding {ECO:0000256|SAAS:SAAS00087792};
Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|SAAS:SAAS00087839};
Reference proteome {ECO:0000313|Proteomes:UP000013063};
Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS01002259,
ECO:0000313|EMBL:ENZ81419.1};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087682};
Zinc {ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460797}.
DOMAIN 130 364 TGT. {ECO:0000259|Pfam:PF01702}.
REGION 92 96 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00168}.
REGION 248 254 RNA binding. {ECO:0000256|HAMAP-
Rule:MF_00168}.
REGION 272 276 RNA binding; important for wobble base 34
recognition. {ECO:0000256|HAMAP-
Rule:MF_00168}.
ACT_SITE 92 92 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00168}.
ACT_SITE 267 267 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00168}.
BINDING 147 147 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00168}.
BINDING 190 190 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00168}.
BINDING 217 217 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00168}.
SEQUENCE 371 AA; 41043 MW; 8BD0984B92682C27 CRC64;
MAAFPFEIKA VEGKARTGVL KTPRGDIRTP AFMPVGTAAT VKAMTVDQVK ATGADIILGN
TYHLMLRPSA ERVARLGGLH KFMRWDKPIL TDSGGFQVMS LSGISKLTEE AVTFSSHVDG
SKHVLTPERS IEIQADLLGS DIVMQLDECV AWPAEEARAR KGMELSARWA RRSKDAFGTR
DTQALFGIQQ GSTFEALRRE SSDRLREIGF DGYAIGGLAV GEGHEAMCEV LDYAPGLLPE
DRPRYLMGVG KPIDLVEAVA RGVDMFDCVL PTRSGRHGQA WTWDGPINLK NAKYAEDESP
LDPDSDCPAS RDYSKAYLRH LFKAEEILGQ VLLSWHNIAF FQALTAAMRA AIAEGRFERF
RREFRARHLS Q


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