QUEA_THET2
ID QUEA_THET2 Reviewed; 345 AA.
AC Q72JS5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000255|HAMAP-Rule:MF_00113};
DE EC=2.4.99.17 {ECO:0000255|HAMAP-Rule:MF_00113};
DE AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000255|HAMAP-Rule:MF_00113};
GN Name=queA {ECO:0000255|HAMAP-Rule:MF_00113}; OrderedLocusNames=TT_C0693;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the
CC 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC epoxyqueuosine (oQ-tRNA). {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-
CC methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:82834;
CC EC=2.4.99.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00113};
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00113}.
CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000255|HAMAP-
CC Rule:MF_00113}.
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DR EMBL; AE017221; AAS81041.1; -; Genomic_DNA.
DR RefSeq; WP_011173135.1; NC_005835.1.
DR PDB; 1WDI; X-ray; 2.10 A; A=1-345.
DR PDBsum; 1WDI; -.
DR AlphaFoldDB; Q72JS5; -.
DR SMR; Q72JS5; -.
DR STRING; 262724.TT_C0693; -.
DR EnsemblBacteria; AAS81041; AAS81041; TT_C0693.
DR GeneID; 3169205; -.
DR KEGG; tth:TT_C0693; -.
DR eggNOG; COG0809; Bacteria.
DR HOGENOM; CLU_039110_1_1_0; -.
DR OMA; YSYGDGM; -.
DR OrthoDB; 368001at2; -.
DR UniPathway; UPA00392; -.
DR EvolutionaryTrace; Q72JS5; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.10.240; -; 1.
DR Gene3D; 3.40.1780.10; -; 1.
DR HAMAP; MF_00113; QueA; 1.
DR InterPro; IPR003699; QueA.
DR InterPro; IPR042118; QueA_dom1.
DR InterPro; IPR042119; QueA_dom2.
DR InterPro; IPR036100; QueA_sf.
DR PANTHER; PTHR30307; PTHR30307; 1.
DR Pfam; PF02547; Queuosine_synth; 1.
DR SUPFAM; SSF111337; SSF111337; 1.
DR TIGRFAMs; TIGR00113; queA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Queuosine biosynthesis; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..345
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000231384"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1WDI"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:1WDI"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:1WDI"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:1WDI"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1WDI"
SQ SEQUENCE 345 AA; 38429 MW; B4C220BF977366AD CRC64;
MEGLEAYDYH LPPEQIAQEG VEPRDMARLM VVYREGPFRV AHKRVRDLPE FLRPGDVLVF
NESKVIPARL LARKPTGGKV EILLVRERSP GLWEALLGPA RKAPPGTRLL LLSPKDLAPV
PGLQAEVVAV EEDGVRLLRF QGDLVAHLEE VGEVPLPPYI KAKIPMERYQ TVYARRPGSV
AAPTAGLHFT PELLERLREM GVELRFLTLH VGPGTFRPVK GDPEKHEMHA EPYAIPEEVA
EAVNRAKAEG RRVVAVGTTV VRALESAYRE GVGVVAGEGE TRLFIRPPYT FKVVDALFTN
FHLPRSTLLM LVAAFLGRER TLEAYRLAVA EGYRFYSLGD AMLIL
