ATGT_HALVD
ID ATGT_HALVD Reviewed; 516 AA.
AC Q9C4M3; D4GTM9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 92.
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}; Synonyms=tgt;
GN OrderedLocusNames=HVO_2001;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=9242689; DOI=10.1074/jbc.272.32.20146;
RA Watanabe M., Matsuo M., Tanaka S., Akimoto H., Asahi S., Nishimura S.,
RA Katze J.R., Hashizume T., Crain P.F., Mccloskey J.A., Okada N.;
RT "Biosynthesis of archaeosine, a novel derivative of 7-deazaguanosine
RT specific to archaeal tRNA, proceeds via a pathway involving base
RT replacement on the tRNA polynucleotide chain.";
RL J. Biol. Chem. 272:20146-20151(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=19478918; DOI=10.1155/2009/428489;
RA El Yacoubi B., Phillips G., Blaby I.K., Haas C.E., Cruz Y., Greenberg J.,
RA de Crecy-Lagard V.;
RT "A Gateway platform for functional genomics in Haloferax volcanii: deletion
RT of three tRNA modification genes.";
RL Archaea 2:211-219(2009).
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, ECO:0000269|PubMed:19478918,
CC ECO:0000269|PubMed:9242689}.
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 ECO:0000269|PubMed:9242689};
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 -!- DISRUPTION PHENOTYPE: Mutants lack the archaeosine modification, but do
CC not show any growth defects. {ECO:0000269|PubMed:19478918}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
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DR EMBL; AB041011; BAB40327.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE04608.1; -; Genomic_DNA.
DR RefSeq; WP_004041882.1; NZ_AOHU01000038.1.
DR AlphaFoldDB; Q9C4M3; -.
DR SMR; Q9C4M3; -.
DR STRING; 309800.C498_05286; -.
DR EnsemblBacteria; ADE04608; ADE04608; HVO_2001.
DR GeneID; 8925787; -.
DR KEGG; hvo:HVO_2001; -.
DR eggNOG; arCOG00989; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR BRENDA; 2.4.2.48; 2561.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000008243; 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; -; 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 Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..516
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_0000247870"
FT REGION 488..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT CONFLICT 238
FT /note="A -> V (in Ref. 1; BAB40327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 56300 MW; EE2987A6A2EF95EB CRC64;
MRDHFELRDG DLAGRIGRLS VPRAGVTVET PALLPVVNPN IDTISPARLE SEFGAEILIT
NSYIIKTNDH LREEALDVGL HEMLDFDGAI MTDSGSFQLA EYGEIDTTTE EILQFQRDIG
TDIATPVDIP TPPDVAREQA EADLEITRQA LADAEAADTG EMLVNAPVQG STYPDLREEA
GRHADATDLD VFPVGAVVPM MNAYRYDDMV DAVAAAKRGL GVDAPVHLFG AGHPMMLALA
VALGCDLFDS AAYALYARDG RYLTVRGTEH LEDLDYLPCT CPICTEYSPD DLREKGSKRQ
EQLLAEHNLH VTFAELRRIK QAIRDGDLME LVEERARSHP AMLDGYRALL AHVDQLERED
PASKGAFFYA SNESAHRPEV ARHHARMDRL TAEGHVLLTE GGVPSGDDFD ATWRVVPPFG
PFPRSLSETY PLTAEVPERL DRDAYEQAAR GVSRLVEENP DAAFTLAHDD WPESALARVP
ESVELESLSA VSERLGDEAS VGGDDGDDGG SASSAE
