(data stored in ACNUC1104 zone)

SWISSPROT: C0ZM75_RHOE4

ID   C0ZM75_RHOE4            Unreviewed;       420 AA.
AC   C0ZM75;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 78.
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   ECO:0000313|EMBL:BAH31052.1};
GN   OrderedLocusNames=RER_03440 {ECO:0000313|EMBL:BAH31052.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31052.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31052.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00168, ECO:0000256|RuleBase:RU003777};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00168, 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP008957; BAH31052.1; -; Genomic_DNA.
DR   STRING; 234621.RER_03440; -.
DR   EnsemblBacteria; BAH31052; BAH31052; RER_03440.
DR   KEGG; rer:RER_03440; -.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000002204; 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; C0ZM75.
DR   SWISS-2DPAGE; C0ZM75.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460875,
KW   ECO:0000313|EMBL:BAH31052.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00101950};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|SAAS:SAAS00460855};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00876991,
KW   ECO:0000313|EMBL:BAH31052.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00168,
KW   ECO:0000256|RuleBase:RU003777, ECO:0000256|SAAS:SAAS00460804};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00168, ECO:0000256|RuleBase:RU003777,
KW   ECO:0000256|SAAS:SAAS00087669}.
FT   DOMAIN       23    410       TGT. {ECO:0000259|Pfam:PF01702}.
FT   REGION      100    104       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00168}.
FT   ACT_SITE    100    100       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   ACT_SITE    309    309       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   METAL       347    347       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       349    349       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       352    352       Zinc. {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   METAL       378    378       Zinc; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00168}.
FT   BINDING     179    179       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     229    229       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00168}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00168}.
SQ   SEQUENCE   420 AA;  46673 MW;  899935B2B61C2926 CRC64;
     MPAVDKRPES IFTIGTRLED RLGRTGTIHT PHGDIATPSF VAVGTKATVK AVLPESMKEL
     GAQSLLANAY HLYLQPGPDI VDEAGGLGKF MNWDGPTFTD SGGFQVMSLG VGFKKVLAME
     AVGVQSDDVI AKGKERLATV DDEGVTFKSH LDGSKHRFTP EVSMQIQHQL GADIMFAFDE
     LTTLLNTRGY QERSVERTQA WAIRCINEHE KLTAERAEKP YQALFGVIQG AQYEDLRRQA
     CRGLESIEGE NGYGFDGYGI GGALEKQNLG TIVRWCNEEL PENKPRHMLG ISEPDDFFVA
     IENGADTFDC VNPSRVARNA AIYVRSGRFN INTSRFRRDF TPIDDECDCY TCANYTRAYI
     HHLFKAKEML ASTLCTIHNE RFTVKLVDDI RASIEGGYFH DFKADMLGKF YAAKTPAPQT
//

If you have problems or comments...

PBIL Back to PBIL home page