TIAS_THEPD
ID TIAS_THEPD Reviewed; 445 AA.
AC A1RXS9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS {ECO:0000255|HAMAP-Rule:MF_01892};
DE Short=tRNA(Ile2)-agm2C synthetase {ECO:0000255|HAMAP-Rule:MF_01892};
DE EC=6.3.4.22 {ECO:0000255|HAMAP-Rule:MF_01892};
DE AltName: Full=tRNA(Ile2) agmatidine synthetase {ECO:0000255|HAMAP-Rule:MF_01892};
GN Name=tiaS {ECO:0000255|HAMAP-Rule:MF_01892}; OrderedLocusNames=Tpen_0604;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
CC -!- FUNCTION: ATP-dependent agmatine transferase that catalyzes the
CC formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34)
CC of tRNA(Ile2), converting the codon specificity from AUG to AUA.
CC {ECO:0000255|HAMAP-Rule:MF_01892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-
CC agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H(+) + 2 phosphate;
CC Xref=Rhea:RHEA:43608, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10626,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58145, ChEBI:CHEBI:82748,
CC ChEBI:CHEBI:83545, ChEBI:CHEBI:456215; EC=6.3.4.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01892};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01892}.
CC -!- SIMILARITY: Belongs to the TiaS family. {ECO:0000255|HAMAP-
CC Rule:MF_01892}.
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DR EMBL; CP000505; ABL78009.1; -; Genomic_DNA.
DR RefSeq; WP_011752274.1; NC_008698.1.
DR AlphaFoldDB; A1RXS9; -.
DR SMR; A1RXS9; -.
DR STRING; 368408.Tpen_0604; -.
DR EnsemblBacteria; ABL78009; ABL78009; Tpen_0604.
DR GeneID; 4601224; -.
DR KEGG; tpe:Tpen_0604; -.
DR eggNOG; arCOG01115; Archaea.
DR HOGENOM; CLU_675459_0_0_2; -.
DR OMA; GMCTTYL; -.
DR OrthoDB; 58019at2157; -.
DR Proteomes; UP000000641; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01892; tRNA_Ile2_agm2C_synt; 1.
DR InterPro; IPR013696; DUF1743.
DR InterPro; IPR024913; tRNA_Ile2__agm2C_synt.
DR Pfam; PF08489; DUF1743; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..445
FT /note="tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS"
FT /id="PRO_0000407305"
FT DNA_BIND 278..349
FT /note="OB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01892"
SQ SEQUENCE 445 AA; 49096 MW; 91E432DAF702476A CRC64;
MGLTSVHVGL DDTDSPLGLC TTFVALAIVR EASRIGAGFA DLPYLVRLNP NVPLKTRGNG
AVAIHFLVEE ELVPRVEEAV VRALDDLSER HGKTDPAAIL VKGDVPRAFR SVYLRALTEF
IPSSYVRSVL ERFKGESVKL LYSRSKRPRG LVGAVASLGA YPLEDYTYEL IVYRSPEERS
ESRDISEDLL LELDRKYRPL VFATYDYSSR RVLAVPHGPD PVIFGLRSLD PEILVNVAVD
VLEKISHAGY LLFKTNQGTS AHLQRYKPVA LVRPYDSVVV RGSVAEKPTV ISGGHVIVNV
CDETGCLQIA FYKETGRLNR VAKLLSRGDL VEVGGGVMKK DGLVLNAEYL RLIKPALNVK
RLNPLCPKCG SRMTSAGKGK GYKCPKCGYR AKEAAKIYRV APRTLEPGTY FQSPSAYRHL
TKPPEILGLR PVDATKVLLS GMWFM