ID A0A377LI53_ECOLX Unreviewed; 364 AA. AC A0A377LI53; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-AUG-2022, entry version 17. DE RecName: Full=tRNA 2-selenouridine synthase {ECO:0000256|HAMAP-Rule:MF_01622}; DE EC=2.9.1.3 {ECO:0000256|HAMAP-Rule:MF_01622}; GN Name=selU {ECO:0000256|HAMAP-Rule:MF_01622, GN ECO:0000313|EMBL:STP52502.1}; GN Synonyms=mnmH {ECO:0000313|EMBL:EFH9618546.1}; GN ORFNames=ELX48_12265 {ECO:0000313|EMBL:TFN65918.1}, F9S83_24560 GN {ECO:0000313|EMBL:EFH9618546.1}, HJU54_003057 GN {ECO:0000313|EMBL:HAI6557679.1}, HNC66_17890 GN {ECO:0000313|EMBL:HAJ6716529.1}, NCTC12950_04044 GN {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|Proteomes:UP000560467, ECO:0000313|Proteomes:UP000573723} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CPW81 {ECO:0000313|EMBL:HAJ6716529.1}, and SCHI0016.S.158 RC {ECO:0000313|EMBL:HAI6557679.1, ECO:0000313|Proteomes:UP000573723}; RX PubMed=30286803; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-150(2018). RN [2] {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. RN [3] {ECO:0000313|EMBL:HAJ6716529.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPW81 {ECO:0000313|EMBL:HAJ6716529.1}, and SCHI0016.S.158 RC {ECO:0000313|EMBL:HAI6557679.1}; RG NCBI Pathogen Detection Project; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:TFN65918.1, ECO:0000313|Proteomes:UP000298449} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=URMC_50 {ECO:0000313|EMBL:TFN65918.1, RC ECO:0000313|Proteomes:UP000298449}; RA Mostafa H., Pecora N.; RT "ESBL Survelliance."; RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:EFH9618546.1, ECO:0000313|Proteomes:UP000547792} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSIS11924176 {ECO:0000313|EMBL:EFH9618546.1, RC ECO:0000313|Proteomes:UP000547792}; RG NARMS: The National Antimicrobial Resistance Monitoring System; RL Submitted (OCT-2019) 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 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:0000256|HAMAP-Rule:MF_01622}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate + 5-methylaminomethyl-2- CC thiouridine(34) in tRNA + H(+) + H2O + selenophosphate = (2E)- CC thiogeraniol + 5-methylaminomethyl-2-selenouridine(34) in tRNA + CC diphosphate + phosphate; 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; EC=2.9.1.3; Evidence={ECO:0000256|HAMAP- CC 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:0000256|HAMAP-Rule:MF_01622}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methylaminomethyl-2-(Se-phospho)selenouridine(34) in tRNA + CC H2O = 5-methylaminomethyl-2-selenouridine(34) in tRNA + phosphate; CC Xref=Rhea:RHEA:60176, Rhea:RHEA-COMP:10196, Rhea:RHEA-COMP:15523, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:82743, CC ChEBI:CHEBI:143702; Evidence={ECO:0000256|HAMAP-Rule:MF_01622}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methylaminomethyl-S-(2E)-geranyl-thiouridine(34) in tRNA + CC H(+) + selenophosphate = (2E)-thiogeraniol + 5-methylaminomethyl-2- CC (Se-phospho)selenouridine(34) in tRNA; Xref=Rhea:RHEA:60172, CC Rhea:RHEA-COMP:14654, Rhea:RHEA-COMP:15523, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16144, ChEBI:CHEBI:140632, ChEBI:CHEBI:143702, CC ChEBI:CHEBI:143703; Evidence={ECO:0000256|HAMAP-Rule:MF_01622}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01622}. CC -!- SIMILARITY: Belongs to the SelU family. {ECO:0000256|HAMAP- CC Rule:MF_01622}. 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; AASXMH010000078; EFH9618546.1; -; Genomic_DNA. DR EMBL; DABFBD010000013; HAI6557679.1; -; Genomic_DNA. DR EMBL; DABIBM010000012; HAJ6716529.1; -; Genomic_DNA. DR EMBL; UGFM01000001; STP52502.1; -; Genomic_DNA. DR EMBL; RZEM01000010; TFN65918.1; -; Genomic_DNA. DR RefSeq; WP_001157971.1; NZ_WTVC01000083.1. DR EnsemblBacteria; STP52502; STP52502; NCTC12950_04044. DR Proteomes; UP000255454; Unassembled WGS sequence. DR Proteomes; UP000298449; Unassembled WGS sequence. DR Proteomes; UP000547792; Unassembled WGS sequence. DR Proteomes; UP000560467; Unassembled WGS sequence. DR Proteomes; UP000573723; 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:UniProtKB-EC. 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; SelU. 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 Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_01622}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01622, ECO:0000313|EMBL:STP52502.1}. FT DOMAIN 14..137 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT ACT_SITE 97 FT /note="S-selanylcysteine intermediate" FT /evidence="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 //