TGT_SCHPO
ID TGT_SCHPO Reviewed; 404 AA.
AC O94460;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_03218};
GN ORFNames=SPAC1687.19c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=24911101; DOI=10.1021/cb500278k;
RA Zallot R., Brochier-Armanet C., Gaston K.W., Forouhar F., Limbach P.A.,
RA Hunt J.F., de Crecy-Lagard V.;
RT "Plant, animal, and fungal micronutrient queuosine is salvaged by members
RT of the DUF2419 protein family.";
RL ACS Chem. Biol. 9:1812-1825(2014).
CC -!- FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:24911101).
CC Catalysis occurs through a double-displacement mechanism. The
CC nucleophile active site attacks the C1' of nucleotide 34 to detach the
CC guanine base from the RNA, forming a covalent enzyme-RNA intermediate.
CC The proton acceptor active site deprotonates the incoming queuine,
CC allowing a nucleophilic attack on the C1' of the ribose to form the
CC product. {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000305|PubMed:24911101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC COMP:10345, ChEBI:CHEBI:16235, ChEBI:CHEBI:74269, ChEBI:CHEBI:77674,
CC ChEBI:CHEBI:82831; EC=2.4.2.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03218, ECO:0000305|PubMed:24911101};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03218};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Lacks queuosine in tRNA(Asp).
CC {ECO:0000269|PubMed:24911101}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
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DR EMBL; CU329670; CAA22613.1; -; Genomic_DNA.
DR PIR; T37762; T37762.
DR RefSeq; NP_593138.1; NM_001018534.2.
DR AlphaFoldDB; O94460; -.
DR SMR; O94460; -.
DR BioGRID; 278609; 3.
DR STRING; 4896.SPAC1687.19c.1; -.
DR MaxQB; O94460; -.
DR PaxDb; O94460; -.
DR EnsemblFungi; SPAC1687.19c.1; SPAC1687.19c.1:pep; SPAC1687.19c.
DR GeneID; 2542133; -.
DR KEGG; spo:SPAC1687.19c; -.
DR PomBase; SPAC1687.19c; -.
DR VEuPathDB; FungiDB:SPAC1687.19c; -.
DR eggNOG; KOG3908; Eukaryota.
DR HOGENOM; CLU_022060_0_1_1; -.
DR InParanoid; O94460; -.
DR OMA; GIDLFDC; -.
DR PhylomeDB; O94460; -.
DR PRO; PR:O94460; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; ISM:PomBase.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IMP:PomBase.
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;
KW Cytoplasm; Glycosyltransferase; Metal-binding; Nucleus; Reference proteome;
KW Transferase; tRNA processing; Zinc.
FT CHAIN 1..404
FT /note="Queuine tRNA-ribosyltransferase catalytic subunit"
FT /id="PRO_0000135569"
FT REGION 253..259
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT REGION 277..281
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 98..102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
SQ SEQUENCE 404 AA; 45176 MW; D192781D8854D4C3 CRC64;
MASSFPALQF KVVARCSTTR ARVTDIQLPH GLVESPVFMP VGTQASLKGV LPEQLDALGC
KIMLNNTYHL GLKPGQEVLD TVGGAHRFQS WNKNILTDSG GFQMVSLLKL ATITEDGVTF
LSPRDGTPML LTPEHSISLQ NSIGSDIMMQ LDDVVHTLTE SKRMEEAMYR SIRWLDRCIQ
AHKRPETQNL FCIIQGGLDK RLREICCREM VKRNTPGIAV GGLSGGEEKH AFCETVYTCT
SILPDNKPRY LMGVGYAEDL VVCVALGMDM FDCVYPTRTA RFGNALTRKG VINLRNQKFR
NDIGPLEEGC SCPCCKTELE GGWGITRAYF NSLVSKETVG ANLMTIHNVH FQLQLMRDMR
ESIIKDEFPS FVKNFFHEWN HGDKSNYPSW AVDALRMVNI DLLA
