(data stored in ACNUC7421 zone)

SWISSPROT: A4AWT5_MARSH

ID   A4AWT5_MARSH            Unreviewed;       358 AA.
AC   A4AWT5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087750};
DE            EC=2.4.2.29 {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087822};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000256|HAMAP-Rule:MF_00168};
GN   OrderedLocusNames=FB2170_00065 {ECO:0000313|EMBL:EAQ99602.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99602.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99602.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue
CC       with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at
CC       position 34 (anticodon wobble position) in tRNAs with GU(N)
CC       anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs
CC       through a double-displacement mechanism. The nucleophile active
CC       site attacks the C1' of nucleotide 34 to detach the guanine base
CC       from the RNA, forming a covalent enzyme-RNA intermediate. The
CC       proton acceptor active site deprotonates the incoming PreQ1,
CC       allowing a nucleophilic attack on the C1' of the ribose to form
CC       the product. After dissociation, two additional enzymatic
CC       reactions on the tRNA convert PreQ1 to queuine (Q), resulting in
CC       the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC       cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
CC       ECO:0000256|SAAS:SAAS00628203}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-
CC         aminomethyl-7-carbaguanosine(34) in tRNA + guanine;
CC         Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC         COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00168,
CC         ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS01115764};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003777};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU003777};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|SAAS:SAAS00087869}.
CC   -!- SUBUNIT: Homodimer. Within each dimer, one monomer is responsible
CC       for RNA recognition and catalysis, while the other monomer binds
CC       to the replacement base PreQ1. {ECO:0000256|HAMAP-Rule:MF_00168,
CC       ECO:0000256|SAAS:SAAS00628204}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
CC       ECO:0000256|SAAS:SAAS00571098}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00168}.
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DR   EMBL; CP002157; EAQ99602.1; -; Genomic_DNA.
DR   STRING; 313603.FB2170_00065; -.
DR   EnsemblBacteria; EAQ99602; EAQ99602; FB2170_00065.
DR   KEGG; fbc:FB2170_00065; -.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR   InterPro; IPR004803; TGT.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AWT5.
DR   SWISS-2DPAGE; A4AWT5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460875};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00101950};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00460855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00876991,
KW   ECO:0000313|EMBL:EAQ99602.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460804};
KW   Zinc {ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00087669}.
FT   DOMAIN        3    354       TGT. {ECO:0000259|Pfam:PF01702}.
FT   REGION       74     78       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      234    240       RNA binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   REGION      258    262       RNA binding; important for wobble base 34
FT                                recognition. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE     74     74       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE    253    253       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     128    128       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     176    176       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     203    203       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00168}.
SQ   SEQUENCE   358 AA;  40933 MW;  B065E0EAF83739FE CRC64;
     MVTDHGVIET PIFMPVGTVA SVKGVHQKEL KEEINPDIIL GNTYHLFLRP KTQILQQAGG
     LHKFMGWDRN ILTDSGGYQV YSLSANRKIK EEGVKFKSHI DGSMHMFTPE NVMEIQRVIG
     ADIIMAFDEC TPYPCDYNYA KRSMHMTHRW LDRCMSHLEK TPFTYDYSQT FFPIVQGSTY
     KDLRKQSAEY IANAGAEGNA IGGLSVGEPA EEMYAMTEVV CEILPEDKPR YLMGVGTPIN
     ILENIALGID MFDCVMPTRN ARNGMLFTAH GTINIKNKKW EDNFSPIDEM GTTFVDREYS
     KAYLRHLFAA NEYLGKQIAT IHNLGFYLWL TREARKHILT GDFTQWKNVM VKQMDKRL
//

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