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SELU_SHIF8
ID   SELU_SHIF8              Reviewed;         364 AA.
AC   Q0T790;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=tRNA 2-selenouridine synthase {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.9.1.3 {ECO:0000255|HAMAP-Rule:MF_01622};
GN   Name=selU {ECO:0000255|HAMAP-Rule:MF_01622}; OrderedLocusNames=SFV_0470;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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 = (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:0000255|HAMAP-
CC         Rule:MF_01622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42717;
CC         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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14086;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60173;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01622};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60177;
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}.
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DR   EMBL; CP000266; ABF02736.1; -; Genomic_DNA.
DR   RefSeq; WP_001157939.1; NC_008258.1.
DR   AlphaFoldDB; Q0T790; -.
DR   SMR; Q0T790; -.
DR   EnsemblBacteria; ABF02736; ABF02736; SFV_0470.
DR   KEGG; sfv:SFV_0470; -.
DR   HOGENOM; CLU_043456_1_0_6; -.
DR   OMA; RPLVYCW; -.
DR   BioCyc; SFLE373384:SFV_RS02600-MON; -.
DR   Proteomes; UP000000659; 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: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; Transferase.
FT   CHAIN           1..364
FT                   /note="tRNA 2-selenouridine synthase"
FT                   /id="PRO_0000292718"
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;  41222 MW;  2E46BE79A16D935D CRC64;
     MQERHTEQDY RALLIADTPI IDVRAPIEFE QGAMPAAINL PLMDNDERAA VGTCYKQQGS
     DAALALGHKL VAGEIRQQRM YAWRAACLQN PQGILCCARG GQRSHIVQRW LHEAGIDYPL
     VEGGYKALRQ TAIQATIELA QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG
     RTLQPQLSQA SFENLLAAEM LKTDARQDLR LWVLEDESRM IGSNHLPECL RERMTQAAIA
     VVEDPFEIRL ERLNEEYFLR MHHDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE
     LAAQLDTALT TQLTTGSTDG HLAWLVPLLK EYYDPMYRYQ LEKKAEKVVF RGEWAEVAVW
     VKAQ
 
 
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