Entry sw:TGT_GLUDA

ID   TGT_GLUDA               Reviewed;         387 AA.
AC   A9HBJ2; B5ZGL7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   30-NOV-2016, entry version 70.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00168};
DE            EC=2.4.2.29 {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_00168};
DE   AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_00168};
GN   Name=tgt {ECO:0000255|HAMAP-Rule:MF_00168};
GN   OrderedLocusNames=GDI0877, Gdia_1142;
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 /
OS   PAl5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / PAl5;
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L.,
RA   Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M.,
RA   Nogueira E., Cidade D., Oliveira D., Simao T., Macedo J., Valadao A.,
RA   Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E.,
RA   Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H.,
RA   Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B.,
RA   Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA   Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E.,
RA   Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P.,
RA   Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E.,
RA   von Kruger W., Martins O., Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / PAl5;
RX   PubMed=21304715; DOI=10.4056/sigs.972221;
RA   Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT   "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT   diazotrophicus PAl 5, suggest a new standard in genome sequence
RT   submission.";
RL   Stand. Genomic Sci. 2:309-317(2010).
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:0000255|HAMAP-Rule:MF_00168}.
CC   -!- CATALYTIC ACTIVITY: Guanine(34) in tRNA + 7-aminomethyl-7-
CC       carbaguanine = 7-aminomethyl-7-carbaguanine(34) in tRNA + guanine.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00168};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00168};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
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:0000255|HAMAP-Rule:MF_00168}.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00168}.
DR   EMBL; AM889285; CAP54820.1; -; Genomic_DNA.
DR   EMBL; CP001189; ACI50925.1; -; Genomic_DNA.
DR   RefSeq; WP_012223664.1; NC_010125.1.
DR   RefSeq; WP_012553616.1; NC_011365.1.
DR   ProteinModelPortal; A9HBJ2; -.
DR   STRING; 272568.GDI_0877; -.
DR   EnsemblBacteria; ACI50925; ACI50925; Gdia_1142.
DR   EnsemblBacteria; CAP54820; CAP54820; GDI0877.
DR   KEGG; gdi:GDI0877; -.
DR   KEGG; gdj:Gdia_1142; -.
DR   PATRIC; 22050652; VBIGluDia203729_1132.
DR   eggNOG; ENOG4105C6U; Bacteria.
DR   eggNOG; COG0343; LUCA.
DR   HOGENOM; HOG000223473; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; POG091H00XO; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000736; Chromosome.
DR   Proteomes; UP000001176; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 1.
DR   HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR   InterPro; IPR004803; Queuine_tRNA-ribosylTrfase.
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;
KW   Complete proteome; Glycosyltransferase; Metal-binding;
KW   Queuosine biosynthesis; Reference proteome; Transferase;
KW   tRNA processing; Zinc.
FT   CHAIN         1    387       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_1000077010.
FT   REGION       93     97       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      248    254       RNA binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   REGION      272    276       RNA binding; important for wobble base 34
FT                                recognition. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   ACT_SITE     93     93       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   ACT_SITE    267    267       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   METAL       305    305       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       307    307       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       310    310       Zinc. {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   METAL       336    336       Zinc; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   BINDING     147    147       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   BINDING     190    190       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00168}.
FT   BINDING     217    217       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00168}.
FT   CONFLICT     13     13       V -> M (in Ref. 2; ACI50925).
FT                                {ECO:0000305}.
FT   CONFLICT    225    225       E -> D (in Ref. 2; ACI50925).
FT                                {ECO:0000305}.
FT   CONFLICT    228    228       Y -> F (in Ref. 2; ACI50925).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       131    359       ipfam:TGT [T]
FT   MYHIT         3    367       ihamap:Q_tRNA_Tgt [T]
SQ   SEQUENCE   387 AA;  42198 MW;  A4B1CCD29B391D07 CRC64;
     MSTAFRWVEQ ARVGRARAGH LHTAHGVVPT PTFMPVGTVG TVKAMTMDSV RSTGAGIVLG
     NTYHLMLRPG AEKVRALGGL HRFMDWPGPI LTDSGGFQVM SLGALRKLDQ DGVTFNSHID
     GSKHRLTPER STDIQHALDA TITMCFDECP ALPAPPETIA QSMRLSMRWA ARCREAFVPR
     AGYAQYGIIQ GGTEPELRAE SVRALTGIGF EGYAIGGLAV GEGQELMYAT LDATVPLIPH
     DSPRYLMGVG TPDDLLGAVE RGVDMFDCVM PTRAGRTARA YTERGTLNLR NARHADDTRP
     LSPHCDCLAC TRHSRAYLHH LFRANEILGP MLLTWHNLAY YQRLMRGMRG AIVAGTLGAH
     AAGLRAEWAM EDWTPDEMPP PDLPPVP
//