位置:首页 > 蛋白库 > QUEA_DEIRA
QUEA_DEIRA
ID   QUEA_DEIRA              Reviewed;         362 AA.
AC   Q9RU19;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=DR_1577;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000513; AAF11138.1; -; Genomic_DNA.
DR   PIR; F75379; F75379.
DR   RefSeq; NP_295300.1; NC_001263.1.
DR   RefSeq; WP_010888216.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RU19; -.
DR   SMR; Q9RU19; -.
DR   STRING; 243230.DR_1577; -.
DR   EnsemblBacteria; AAF11138; AAF11138; DR_1577.
DR   KEGG; dra:DR_1577; -.
DR   PATRIC; fig|243230.17.peg.1780; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_1_0; -.
DR   InParanoid; Q9RU19; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 368001at2; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000002524; Chromosome I.
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   3: Inferred from homology;
KW   Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..362
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000165399"
SQ   SEQUENCE   362 AA;  39562 MW;  FD45EACAF59A3B2F CRC64;
     MPDSTADPST ADEVLARLHF DLPEDRIAQT GAEPRDTSRL MVVGEQIKHR MFRDLPDLLR
     PSDLLVFNES RVIPARVLAR KPVVNGFGGG QVEVLLLREE FDVGANVWSA YLKPAKRAGH
     ELWLGENEAT GHRAEVVGVL DDGARLLRFD HDIKPHLDEI GRLPLPPYIN AGDSDETWRE
     RYQTVYAKTP GSVAAPTAGL HFTPELLARL DEMGVERASV TLHVGAGTFK PIQGPVADHV
     MHAERYEVSE TNAAAITRAK AEGRRVVAVG TTTVRTLESA WDGAAVRAGA GETRIFITPG
     TRVEVPDLLI TNLHLPGSTL LLLVAAFAGE DRIRAAYDAA LSQDYRFYSL GDAMLLERLT
     SA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024