ID A0A377LI53_ECOLX Unreviewed; 364 AA. AC A0A377LI53; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 31-JUL-2019, entry version 6. DE RecName: Full=tRNA 2-selenouridine synthase {ECO:0000256|HAMAP-Rule:MF_01622, ECO:0000256|SAAS:SAAS00356057}; DE EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01622, ECO:0000256|SAAS:SAAS01064486}; GN Name=selU {ECO:0000256|HAMAP-Rule:MF_01622, GN ECO:0000313|EMBL:STP52502.1}; GN ORFNames=NCTC12950_04044 {ECO:0000313|EMBL:STP52502.1}; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562 {ECO:0000313|EMBL:STP52502.1, ECO:0000313|Proteomes:UP000255454}; RN [1] {ECO:0000313|EMBL:STP52502.1, ECO:0000313|Proteomes:UP000255454} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC12950 {ECO:0000313|EMBL:STP52502.1, RC ECO:0000313|Proteomes:UP000255454}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. 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 CC 2-selenouridine (Se2U-RNA). Acts in a two-step process involving CC geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine CC (geS2U) and subsequent selenation of the latter derivative to 2- CC selenouridine (Se2U) in the tRNA chain. {ECO:0000256|HAMAP- CC Rule:MF_01622}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate + 5-methylaminomethyl-2- CC thiouridine(34) in tRNA + H(+) + H2O + selenophosphate = (2E)- CC 3,7-dimethylocta-2,6-diene-1-thiol + 5-methylaminomethyl-2- CC selenouridine(34) in tRNA + diphosphate + phosphate; CC Xref=Rhea:RHEA:42716, Rhea:RHEA-COMP:10195, Rhea:RHEA- CC 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:0000256|HAMAP-Rule:MF_01622}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01622, CC ECO:0000256|SAAS:SAAS00356061}. CC -!- SIMILARITY: Belongs to the SelU family. {ECO:0000256|HAMAP- CC Rule:MF_01622, ECO:0000256|SAAS:SAAS01064488}. 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; UGFM01000001; STP52502.1; -; Genomic_DNA. DR RefSeq; WP_001157971.1; NZ_UIJJ01000024.1. DR Proteomes; UP000255454; Unassembled WGS sequence. 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; KW Complete proteome {ECO:0000313|Proteomes:UP000255454}; KW Selenium {ECO:0000256|HAMAP-Rule:MF_01622, KW ECO:0000256|SAAS:SAAS00433829}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01622, KW ECO:0000256|SAAS:SAAS00433820, ECO:0000313|EMBL:STP52502.1}. FT DOMAIN 14 137 Rhodanese. {ECO:0000259|PROSITE:PS50206}. FT ACT_SITE 97 97 S-selanylcysteine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01622}. SQ SEQUENCE 364 AA; 41210 MW; E2B5C9074A8C6609 CRC64; MQERHTEQDY RALLIADTPI IDVRAPIEFE QGAMPAAINL PLMNNDERAA VGTCYKQQGS DAALALGHKL VAGEIRQQRM DAWRAACLQN PQGILCCARG GQRSHIVQRW LHEAGIDYPL VDGGYKALRQ TAIQATIELS QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG RTLQPQLSQA SFENLLAAEM LKTDARQDLH LWVLEDESRM IGSNHLPECL RERMTQAAIA VVEDPFEIRL ERLNEEYFLR MHYDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE LAARLDAALA TQLTTGSTDG HLAWLVPLLK EYYDPMYRYQ LEKKAEKVVF RGEWAEVAEW VKTQ //