ATGT_METMP
ID ATGT_METMP Reviewed; 649 AA.
AC Q6LZL5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
DE EC=2.4.2.48 {ECO:0000255|HAMAP-Rule:MF_01634};
DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01634};
DE AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
GN Name=tgtA {ECO:0000255|HAMAP-Rule:MF_01634}; OrderedLocusNames=MMP0610;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
CC -!- FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine
CC (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal
CC tRNAs. {ECO:0000255|HAMAP-Rule:MF_01634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-
CC carbaguanosine(15) in tRNA + guanine; Xref=Rhea:RHEA:43164,
CC Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:10372, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:45075, ChEBI:CHEBI:74269, ChEBI:CHEBI:82850; EC=2.4.2.48;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01634};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
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DR EMBL; BX950229; CAF30166.1; -; Genomic_DNA.
DR RefSeq; WP_011170554.1; NC_005791.1.
DR AlphaFoldDB; Q6LZL5; -.
DR SMR; Q6LZL5; -.
DR STRING; 267377.MMP0610; -.
DR PRIDE; Q6LZL5; -.
DR EnsemblBacteria; CAF30166; CAF30166; MMP0610.
DR GeneID; 2762310; -.
DR KEGG; mmp:MMP0610; -.
DR PATRIC; fig|267377.15.peg.624; -.
DR eggNOG; arCOG00989; Archaea.
DR eggNOG; arCOG00991; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR BioCyc; MMAR267377:MMP_RS03210-MON; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.10.450.90; -; 1.
DR Gene3D; 3.20.20.105; -; 1.
DR Gene3D; 3.90.1020.10; -; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR038370; ArcTGT_C1_sf.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR029402; TGT_C2.
DR InterPro; IPR038250; TGT_C2_sf.
DR InterPro; IPR004804; TgtA.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF14810; TGT_C2; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..649
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247871"
FT DOMAIN 573..648
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ SEQUENCE 649 AA; 74401 MW; FA2227F96B4925DC CRC64;
MFEIKARDAM GRLGSITING KKIETPTIMP VIHPNPKKQT VSMDLINKMA DVVITNSYIT
YTTPELREIA ETKGIHELID FKNVVVTDSG SFQLSVYGDV NVGPMEIIDF QEKIGVDVGT
ILDIPTGPDV SREKAESDLI ETFKRAEDSI KRRKEMGYKL ALNGTIQGSK YLDLRQKSAE
VMGKMDFDIY PIGAVVPLME DYRYREVAEV ILNSKMHLPT NKPVHLFGCG HPMLFALSVA
LGCDLFDSAA YALYAKNGRY LTADGTLHLK DMKDLKSFPC TCKVCSEYTP KQLYNLEEKE
KTRLLAEHNL YVTFEEIDRI KNAIKEGNLW ELVEERCRSH PKLLNGLRVI SKYMDFIEKH
DPVSKKSGFF YTGYESMNRP EIYRHKQRLD RIQYDKIYVT SVSENTSKPY SENLSNVPCD
VDVLVKDSVF GLVPLNIDTM YPLAQNEVPD LYDFEKKYNN EFVSEFNEKH AEKILDISTY
NYYINHYGKK KECDKINPDI FRIGKMLEYQ YGAKILDEEL MEKVKSRRSK NTGRIRNLLL
EKEVLFTLRA NDNFLIPAKS GAELLHEKLE FPKYRIVIDS SVEEFARAGK SVYSKFVKDC
DPELRPFEEV LIVNSDDELL AYGTTILNGR ELMEFDYGVA ATLRGGLKK
