(data stored in ACNUC7421 zone)

SWISSPROT: QUEA_RHILO

ID   QUEA_RHILO              Reviewed;         361 AA.
AC   Q98M55;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 88.
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=mll0724;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
DR   EMBL; BA000012; BAB48258.1; -; Genomic_DNA.
DR   RefSeq; WP_010909613.1; NC_002678.2.
DR   SMR; Q98M55; -.
DR   STRING; 266835.14021646; -.
DR   PRIDE; Q98M55; -.
DR   EnsemblBacteria; BAB48258; BAB48258; BAB48258.
DR   KEGG; mlo:mll0724; -.
DR   PATRIC; fig|266835.9.peg.582; -.
DR   eggNOG; ENOG4105E2N; Bacteria.
DR   eggNOG; COG0809; LUCA.
DR   HOGENOM; HOG000004401; -.
DR   KO; K07568; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 368001at2; -.
DR   BioCyc; MLOT266835:G1G20-596-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; Q98M55.
DR   SWISS-2DPAGE; Q98M55.
KW   Cytoplasm; Queuosine biosynthesis; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..361
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000165430"
SQ   SEQUENCE   361 AA;  39380 MW;  75AF00C1C2A72B50 CRC64;
     MRVDLFDFEL PEERIALRPA EPRDSAKMLV VKSGEALDDR KVGDLPSLLR AGDVLVFNDT
     KVIPAQLKGI RRRGEAQAQV EATLHMRVAP DRWLAFMRPG KRIAAGDRIH FGHDGNSCFL
     GQLDATVIEK GEGGEALLGF DLSGPFLDEA LHAVGHIPLP PYIASKRDDD ERDRADYQTI
     YAREEGAVAA PTAGLHFTPE LFAALDAKGV ERHFVTLHVG AGTFLPVKAD DTADHKMHAE
     IGSVSRETAD ALNAAKARGG RIIAVGTTSL RLLESAARED GTVPAWSGPT DIFITPGYRF
     RTADMLMTNF HLPRSTLFML VSAFSGLDTM GAAYAHAIAN RYRFYSYGDA SLLYRAEMSD
     G
//

If you have problems or comments...

PBIL Back to PBIL home page