QUEA_THEMA
ID QUEA_THEMA Reviewed; 335 AA.
AC Q9WZ44;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase;
DE EC=2.4.99.17;
DE AltName: Full=Queuosine biosynthesis protein QueA;
GN Name=queA; OrderedLocusNames=TM_0574;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=15822125; DOI=10.1002/prot.20419;
RA Mathews I., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E.,
RA Axelrod H., Biorac T., Canaves J.M., Chiu H.-J., Deacon A.M., DiDonato M.,
RA Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hale J.,
RA Hampton E., Han G.W., Haugen J., Hornsby M., Jaroszewski L., Klock H.E.,
RA Koesema E., Kreusch A., Kuhn P., Lesley S.A., Levin I., Miller M.D.,
RA Moy K., Nigoghossian E., Ouyang J., Paulsen J., Quijano K., Reyes R.,
RA Spraggon G., Stevens R.C., van den Bedem H., Velasquez J., Vincent J.,
RA White A., Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-
RT isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new
RT fold.";
RL Proteins 59:869-874(2005).
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:0000250}.
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;
CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15822125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the QueA family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35659.1; -; Genomic_DNA.
DR PIR; A72360; A72360.
DR RefSeq; NP_228384.1; NC_000853.1.
DR RefSeq; WP_004081288.1; NZ_CP011107.1.
DR PDB; 1VKY; X-ray; 2.00 A; A/B=1-335.
DR PDBsum; 1VKY; -.
DR AlphaFoldDB; Q9WZ44; -.
DR SMR; Q9WZ44; -.
DR STRING; 243274.THEMA_01800; -.
DR EnsemblBacteria; AAD35659; AAD35659; TM_0574.
DR KEGG; tma:TM0574; -.
DR eggNOG; COG0809; Bacteria.
DR InParanoid; Q9WZ44; -.
DR OMA; LSKHKMD; -.
DR OrthoDB; 368001at2; -.
DR BRENDA; 2.4.99.17; 6331.
DR UniPathway; UPA00392; -.
DR EvolutionaryTrace; Q9WZ44; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IBA:GO_Central.
DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
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; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..335
FT /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT isomerase"
FT /id="PRO_0000165458"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1VKY"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:1VKY"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:1VKY"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1VKY"
SQ SEQUENCE 335 AA; 38662 MW; 8D634537041B13E9 CRC64;
MKVSEFDYEL PPELIAQEPV EPRDASRLMV LHRKTQRIEH RIFREIIEYL EPGDLLVLNV
SKVIPARLYA RKKTGASIEI LLIERLEEGI WKCLVRPGQK VKKGTELVID EDLSAVCLGR
GEDGTRILKF QPQDDRLIFE KGRTPLPPYI KNEVPLERYQ TVYAKEEGSV AAPTAGLHFT
PELIEKLKKK GVQFAEVVLH VGIGTFRPVK VEEVEKHKMH EEFYQVPKET VRKLRETRER
GNRIVAVGTT TVRTLETIAR LPEQEEYVGK TDLFIYPPFE FKLVDALVTN FHLPRSTLLM
LVAAFAGKDF VMEAYREAVK RRYRFFSFGD AMLIL
