(data stored in ACNUC7421 zone)

SWISSPROT: SELU_ECO27

ID   SELU_ECO27              Reviewed;         364 AA.
AC   B7UKI1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=tRNA 2-selenouridine/geranyl-2-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.9.1.- {ECO:0000255|HAMAP-Rule:MF_01622};
GN   Name=selU {ECO:0000255|HAMAP-Rule:MF_01622};
GN   OrderedLocusNames=E2348C_0437;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Involved in the post-transcriptional modification of the
CC       uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and
CC       tRNA(Gln). Catalyzes the selenation and geranylation of 2-
CC       thiouridine, forming 5-methylaminomethyl-2-selenouridine
CC       (mnm5Se2U) and geranylated 5-methylaminomethyl-2-thiouridine
CC       (mnm5ges2U), respectively. The two reactions may occur
CC       independently or in a linear manner, where S-geranyl-2-thiouridine
CC       is an intermediate of the conversion of 2-thiouridine to 2-
CC       selenouridine. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) +
CC         selenophosphate = 5-methylaminomethyl-2-selenouridine(34) in
CC         tRNA + thiophosphate; Xref=Rhea:RHEA:42716, Rhea:RHEA-
CC         COMP:10195, Rhea:RHEA-COMP:10196, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:74455, ChEBI:CHEBI:74752,
CC         ChEBI:CHEBI:82743; Evidence={ECO:0000255|HAMAP-Rule:MF_01622};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + 5-methylaminomethyl-2-
CC         thiouridine(34) in tRNA = 5-methylaminomethyl-S-(2E)-geranyl-
CC         thiouridine(34) in tRNA + diphosphate; Xref=Rhea:RHEA:14085,
CC         Rhea:RHEA-COMP:10195, Rhea:RHEA-COMP:14654, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057, ChEBI:CHEBI:74455, ChEBI:CHEBI:140632;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01622};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- SIMILARITY: Belongs to the SelU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01622}.
DR   EMBL; FM180568; CAS07985.1; -; Genomic_DNA.
DR   RefSeq; WP_001157956.1; NC_011601.1.
DR   SMR; B7UKI1; -.
DR   EnsemblBacteria; CAS07985; CAS07985; E2348C_0437.
DR   KEGG; ecg:E2348C_0437; -.
DR   KO; K06917; -.
DR   OMA; RPLVYCW; -.
DR   BioCyc; ECOL574521:E2348C_RS02295-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-UniRule.
DR   GO; GO:0043828; F:tRNA 2-selenouridine synthase activity; IEA:InterPro.
DR   GO; GO:0070329; P:tRNA seleno-modification; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.250.10; -; 1.
DR   HAMAP; MF_01622; tRNA_sel_U_synth; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR017582; tRNA_2-selenouridine_synthase.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   TIGRFAMs; TIGR03167; tRNA_sel_U_synt; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKI1.
DR   SWISS-2DPAGE; B7UKI1.
KW   Complete proteome; Selenium; Transferase.
FT   CHAIN         1    364       tRNA 2-selenouridine/geranyl-2-
FT                                thiouridine synthase.
FT                                /FTId=PRO_1000186065.
FT   DOMAIN       14    137       Rhodanese. {ECO:0000255|HAMAP-
FT                                Rule:MF_01622}.
FT   ACT_SITE     97     97       S-selanylcysteine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01622}.
SQ   SEQUENCE   364 AA;  41246 MW;  5CDDE4DA54AF002F CRC64;
     MQERHTEQDY RALLIADTPI IDVRAPIEFE QGAMPAAINL PLMNNDERAA VGICYKQQGS
     DAALAQGHKL VAGEIRQQRM DAWRAACLQN PHGILCCARG GQRSHIVQRW LHDAGIDYPL
     VEGGYKALRQ TAIQATIELA QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG
     RTLQPQLSQA SFENLLAAEM LKTDAHQDLR LWVLEDESRM IGSNHLPECL RERMTQATIA
     VVEDPFEIRL ERLNEEYFLR MHHDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE
     LAARLDAALT TQLTTGSTDG HLAWLVPLLE EYYDPMYRYQ LEKKAEKVVF HGEWAEVAEW
     VKTQ
//

If you have problems or comments...

PBIL Back to PBIL home page