(data stored in SCRATCH zone)

SWISSPROT: A0LFR1_SYNFM

ID   A0LFR1_SYNFM            Unreviewed;       357 AA.
AC   A0LFR1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase {ECO:0000256|HAMAP-Rule:MF_00113, ECO:0000256|SAAS:SAAS00958187};
DE            EC=2.4.99.17 {ECO:0000256|HAMAP-Rule:MF_00113, ECO:0000256|SAAS:SAAS00958171};
DE   AltName: Full=Queuosine biosynthesis protein QueA {ECO:0000256|HAMAP-Rule:MF_00113};
GN   Name=queA {ECO:0000256|HAMAP-Rule:MF_00113};
GN   OrderedLocusNames=Sfum_0564 {ECO:0000313|EMBL:ABK16263.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16263.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16263.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet
CC       to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC       epoxyqueuosine (oQ-tRNA). {ECO:0000256|HAMAP-Rule:MF_00113,
CC       ECO:0000256|SAAS:SAAS00958175}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-
CC         L-methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342,
CC         Rhea:RHEA-COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:82833,
CC         ChEBI:CHEBI:82834; EC=2.4.99.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00113, ECO:0000256|SAAS:SAAS01116098};
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00113, ECO:0000256|SAAS:SAAS00958180}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00113,
CC       ECO:0000256|SAAS:SAAS00958162}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00113,
CC       ECO:0000256|SAAS:SAAS00958183}.
CC   -!- SIMILARITY: Belongs to the QueA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00113, ECO:0000256|SAAS:SAAS00958161}.
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; CP000478; ABK16263.1; -; Genomic_DNA.
DR   RefSeq; WP_011697436.1; NC_008554.1.
DR   STRING; 335543.Sfum_0564; -.
DR   EnsemblBacteria; ABK16263; ABK16263; Sfum_0564.
DR   KEGG; sfu:Sfum_0564; -.
DR   eggNOG; ENOG4105E2N; Bacteria.
DR   eggNOG; COG0809; LUCA.
DR   HOGENOM; HOG000004401; -.
DR   KO; K07568; -.
DR   OMA; YSYGDGM; -.
DR   OrthoDB; 368001at2; -.
DR   BioCyc; SFUM335543:G1G7I-579-MONOMER; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001784; 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; -; 2.
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; A0LFR1.
DR   SWISS-2DPAGE; A0LFR1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958179};
KW   Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958172};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00113,
KW   ECO:0000256|SAAS:SAAS00958166}.
SQ   SEQUENCE   357 AA;  40041 MW;  F1C5A9531A5D7974 CRC64;
     MADERISYRL REYDYDLPPS LIAQSPLSRR EESRLLVLDR GRGAMDHVRF RDLPDHLHAE
     DLLVVNDTRV VPARLIGFKD SGGRIELLVT EPYKSEAEGR RDGYWCLAAA AKRTRPGCLI
     SLPDGTVAEV LEAGDGGRIR VRFPDDRPLM TILSEIGAVP LPPYINRSGT GDFPGDAEAY
     QTVYARNPGA VAAPTAGLHF SSALLEAVAR AGVEVVRITL HVGYGTFAPI RVDDIRDHEM
     HPEYVRVDED STERIRSAID RKRRIVAVGT TVVRSLEWIA HRRGEIMPAA GACAHYIYPG
     YRFKVVDAMI TNFHLPRSSL LLLVSAFAGR RRILEAYREA IRREYRFFSY GDAMLIL
//

If you have problems or comments...

PBIL Back to PBIL home page