ID F4BVU8_METSG Unreviewed; 479 AA.
AC F4BVU8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000256|HAMAP-Rule:MF_01634};
DE EC=2.4.2.48 {ECO:0000256|HAMAP-Rule:MF_01634};
DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01634};
DE AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_01634};
GN Name=tgtA {ECO:0000256|HAMAP-Rule:MF_01634};
GN OrderedLocusNames=MCON_0339 {ECO:0000313|EMBL:AEB67208.1};
OS Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC
OS 103675 / OCM 69 / GP-6) (Methanosaeta concilii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=990316 {ECO:0000313|EMBL:AEB67208.1, ECO:0000313|Proteomes:UP000007807};
RN [1] {ECO:0000313|EMBL:AEB67208.1, ECO:0000313|Proteomes:UP000007807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6
RC {ECO:0000313|Proteomes:UP000007807};
RX PubMed=21571998; DOI=10.1128/JB.05031-11;
RA Barber R.D., Zhang L., Harnack M., Olson M.V., Kaul R., Ingram-Smith C.,
RA Smith K.S.;
RT "Complete genome sequence of Methanosaeta concilii, a specialist in
RT aceticlastic methanogenesis.";
RL J. Bacteriol. 193:3668-3669(2011).
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:0000256|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:0000256|HAMAP-Rule:MF_01634};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01634};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01634};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01634}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_01634}.
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; CP002565; AEB67208.1; -; Genomic_DNA.
DR RefSeq; WP_013718270.1; NC_015416.1.
DR AlphaFoldDB; F4BVU8; -.
DR STRING; 990316.MCON_0339; -.
DR GeneID; 10460104; -.
DR KEGG; mcj:MCON_0339; -.
DR HOGENOM; CLU_030083_0_0_2; -.
DR InParanoid; F4BVU8; -.
DR OrthoDB; 6871at2157; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000007807; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR004804; TgtA.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00432; arcsn_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF88802; Pre-PUA domain; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01634}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01634};
KW Reference proteome {ECO:0000313|Proteomes:UP000007807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01634};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01634}; Zinc {ECO:0000256|HAMAP-Rule:MF_01634}.
FT DOMAIN 14..334
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
SQ SEQUENCE 479 AA; 53531 MW; 7DABACA2ED662516 CRC64;
MPDRFEILHK DLAGRIGRLS TLHGTVETPL LMPVINPHLP LIPPDELASM GAEMVITNSY
IINQDPDLRE GAIEQGLHHL LGFPGPIMTD SGAFQLSVYG DIDVLPLEIL DFQFAIKSDI
SVPLDIPTPP DVSRERAESE LNITEERLRE AAGLKRDALL AGPVQGSTYP DLRERAGRFA
RELGFDLYPI GGVVPLMEAY RFRDLVDVVV SAKKGLGSGV PVHLFGAGHP MIFALAAAMG
CDLFDSAAYA LYAREGRYLT VQGTRKLEEM KHLPCSCPVC LKYTQQELMD SPQRSRELAR
HNLYVSLQEI KLVRQSIRDG SLWDLLETRC RSHPRMLDGL KRLASYGDWL EGLDSASKST
FFYLSPESAS RPEVIRHGRR IERISLKGEV LITDDPNANP SGYDNVLNFK PPFGPYPTQL
SETYPFNAEV PAEADDAAID RAVRITRRLI EANPDARFTF RLKINLEERL EQLPKVHMP
//
