(data stored in SCRATCH3701 zone)

SWISSPROT: SELU_ECOBW

ID   SELU_ECOBW              Reviewed;         364 AA.
AC   C4ZUV3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=tRNA 2-selenouridine synthase {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01622};
GN   Name=selU {ECO:0000255|HAMAP-Rule:MF_01622}; OrderedLocusNames=BWG_0380;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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 conversion of 2-thiouridine (S2U-RNA) to 2-
CC       selenouridine (Se2U-RNA). Acts in a two-step process involving
CC       geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U)
CC       and subsequent selenation of the latter derivative to 2-selenouridine
CC       (Se2U) in the tRNA chain. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate + 5-methylaminomethyl-2-
CC         thiouridine(34) in tRNA + H(+) + H2O + selenophosphate = 5-
CC         methylaminomethyl-2-selenouridine(34) in tRNA + diphosphate +
CC         phosphate + thiogeraniol; Xref=Rhea:RHEA:42716, Rhea:RHEA-COMP:10195,
CC         Rhea:RHEA-COMP:10196, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58057, ChEBI:CHEBI:74455, ChEBI:CHEBI:82743,
CC         ChEBI:CHEBI:143703; Evidence={ECO:0000255|HAMAP-Rule:MF_01622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42717;
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; CP001396; ACR65707.1; -; Genomic_DNA.
DR   RefSeq; WP_001157938.1; NC_012759.1.
DR   SMR; C4ZUV3; -.
DR   PRIDE; C4ZUV3; -.
DR   EnsemblBacteria; ACR65707; ACR65707; BWG_0380.
DR   KEGG; ebw:BWG_0380; -.
DR   HOGENOM; HOG000260000; -.
DR   KO; K06917; -.
DR   OMA; RPLVYCW; -.
DR   BioCyc; ECOL595496:BWG_RS02120-MONOMER; -.
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; C4ZUV3.
DR   SWISS-2DPAGE; C4ZUV3.
KW   Selenium; Transferase.
FT   CHAIN           1..364
FT                   /note="tRNA 2-selenouridine synthase"
FT                   /id="PRO_1000215741"
FT   DOMAIN          14..137
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01622"
FT   ACT_SITE        97
FT                   /note="S-selanylcysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01622"
SQ   SEQUENCE   364 AA;  41111 MW;  8C0F244BA86B6C4A CRC64;
     MQERHTEQDY RALLIADTPI IDVRAPIEFE HGAMPAAINL PLMNNDERAA VGTCYKQQGS
     DAALALGHKL VAGEIRQQRM DAWRAACLQN PQGILCCARG GQRSHIVQSW LHAAGIDYPL
     VEGGYKALRQ TAIQATIELA QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG
     RTLQPQLSQA SFENLLAAEM LKTDARQNLR LWVLEDESRM IGSNHLPECL RERMTQAAIA
     VVEDPFEIRL ERLNEEYFLR MHHDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE
     LAARLDAALT TQLTTGSTDG HLAWLVPLLE EYYDPMYRYQ LEKKAEKVVF RGEWAEVAEW
     VKAR
//

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