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

 F7XV01_MIDMI            Unreviewed;       353 AA.
F7XV01;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
07-JUN-2017, entry version 47.
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,
ECO:0000313|EMBL:AEI88500.1};
OrderedLocusNames=midi_00180 {ECO:0000313|EMBL:AEI88500.1};
Midichloria mitochondrii (strain IricVA).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Candidatus Midichloriaceae; Candidatus Midichloria.
NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88500.1, ECO:0000313|Proteomes:UP000006639};
[1] {ECO:0000313|EMBL:AEI88500.1, ECO:0000313|Proteomes:UP000006639}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IricVA {ECO:0000313|EMBL:AEI88500.1,
ECO:0000313|Proteomes:UP000006639};
PubMed=21690562; DOI=10.1093/molbev/msr159;
Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
"Phylogenomic evidence for the presence of a flagellum and cbb3
oxidase in the free-living mitochondrial ancestor.";
Mol. Biol. Evol. 28:3285-3296(2011).
-!- 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:SAAS00571098}.
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EMBL; CP002130; AEI88500.1; -; Genomic_DNA.
RefSeq; WP_013950716.1; NC_015722.1.
STRING; 696127.midi_00180; -.
EnsemblBacteria; AEI88500; AEI88500; midi_00180.
KEGG; mmn:midi_00180; -.
eggNOG; ENOG4105C6U; Bacteria.
eggNOG; COG0343; LUCA.
KO; K00773; -.
OMA; TYHLFLR; -.
OrthoDB; POG091H00XO; -.
UniPathway; UPA00392; -.
Proteomes; UP000006639; Chromosome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-HAMAP.
GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP.
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; 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:UP000006639};
Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087634,
ECO:0000313|EMBL:AEI88500.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|SAAS:SAAS00087792};
Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087839};
Reference proteome {ECO:0000313|Proteomes:UP000006639};
Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087634,
ECO:0000313|EMBL:AEI88500.1};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087682};
Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
ECO:0000256|SAAS:SAAS00460797}.
DOMAIN 129 351 TGT. {ECO:0000259|Pfam:PF01702}.
REGION 91 95 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00168}.
REGION 246 252 RNA binding. {ECO:0000256|HAMAP-
Rule:MF_00168}.
REGION 270 274 RNA binding; important for wobble base 34
recognition. {ECO:0000256|HAMAP-
Rule:MF_00168}.
ACT_SITE 91 91 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00168}.
ACT_SITE 265 265 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00168}.
METAL 303 303 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
METAL 305 305 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
METAL 308 308 Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
METAL 334 334 Zinc; via pros nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00168}.
BINDING 145 145 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00168}.
BINDING 188 188 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00168}.
BINDING 215 215 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00168}.
SEQUENCE 353 AA; 39669 MW; 5098E6F0BB3CBE3B CRC64;
MAVKFTLIKE VGKTRVGFIE TAHGVINTPA FMPVGTLAAV KAMTPDAISS TGTEIVLSNT
YHLMLRPGED RIERLGGLHK FMNWQKPILT DSGGFQVMSL ASLRKVTEEG VMFRSHIDGH
KYNLTPEYSI QIQHKLGSTI TMAFDECIPY PATFQEAKRA MELSMRWALR SKNSYQNKDG
YGIFAIVQGS AYQELRESSA NFLSAIDFDG YAIGGLAVGE PQAVMFDVLD YTIPLLPKFK
PRYLMGVGKP SDVVGAVERG VDMFDCVIPT RSGRNGQAFV RNGTINIRNA QYVEDIRPLD
SECSCYTCSN FHRAYLRHLV RAKEILGSIL MTWHNIHYYQ DLMKELREKI IRS


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