UniProt functional annotation for P28720



	UniProt functional annotation for P28720

UniProt code: P28720.

Organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).

Taxonomy: Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Zymomonas.

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:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:7665516}.

Catalytic activity: Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7- aminomethyl-7-carbaguanosine(34) in tRNA + guanine; Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000255|HAMAP- Rule:MF_00168, ECO:0000269|PubMed:7665516};

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936};

Biophysicochemical properties: Kinetic parameters: KM=0.2 uM for tRNA(Tyr) {ECO:0000269|PubMed:7665516}; KM=0.7 uM for guanine {ECO:0000269|PubMed:7665516}; Note=kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates. {ECO:0000269|PubMed:7665516};

Pathway: tRNA modification; tRNA-queuosine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:7665516}.

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:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:19627989}.

Similarity: Belongs to the queuine tRNA-ribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_00168}.

Sequence caution: Sequence=AAA27704.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=AAA27705.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=AAG29862.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=Z11910; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
Taxonomy:		Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Zymomonas.



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:0000255\|HAMAP-Rule:MF_00168, ECO:0000269\|PubMed:7665516}.


Catalytic activity:		Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7- aminomethyl-7-carbaguanosine(34) in tRNA + guanine; Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000255\|HAMAP- Rule:MF_00168, ECO:0000269\|PubMed:7665516};
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255\|HAMAP-Rule:MF_00168, ECO:0000269\|PubMed:10413112, ECO:0000269\|PubMed:11178905, ECO:0000269\|PubMed:11921407, ECO:0000269\|PubMed:12646024, ECO:0000269\|PubMed:12909636, ECO:0000269\|PubMed:12949492, ECO:0000269\|PubMed:14523925, ECO:0000269\|PubMed:19627989, ECO:0000269\|PubMed:8654383, ECO:0000269\|PubMed:8961936}; Note=Binds 1 zinc ion per subunit. {ECO:0000255\|HAMAP-Rule:MF_00168, ECO:0000269\|PubMed:10413112, ECO:0000269\|PubMed:11178905, ECO:0000269\|PubMed:11921407, ECO:0000269\|PubMed:12646024, ECO:0000269\|PubMed:12909636, ECO:0000269\|PubMed:12949492, ECO:0000269\|PubMed:14523925, ECO:0000269\|PubMed:19627989, ECO:0000269\|PubMed:8654383, ECO:0000269\|PubMed:8961936};
Biophysicochemical properties:		Kinetic parameters: KM=0.2 uM for tRNA(Tyr) {ECO:0000269\|PubMed:7665516}; KM=0.7 uM for guanine {ECO:0000269\|PubMed:7665516}; Note=kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates. {ECO:0000269\|PubMed:7665516};
Pathway:		tRNA modification; tRNA-queuosine biosynthesis. {ECO:0000255\|HAMAP-Rule:MF_00168, ECO:0000305\|PubMed:7665516}.
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:0000255\|HAMAP-Rule:MF_00168, ECO:0000269\|PubMed:12949492, ECO:0000269\|PubMed:19627989}.
Similarity:		Belongs to the queuine tRNA-ribosyltransferase family. {ECO:0000255\|HAMAP-Rule:MF_00168}.
Sequence caution:		Sequence=AAA27704.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=AAA27705.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=AAG29862.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=Z11910; Type=Frameshift; Evidence={ECO:0000305};