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SELU_SHEFN
ID   SELU_SHEFN              Reviewed;         366 AA.
AC   Q089T3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Sfri_0119;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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: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; CP000447; ABI69982.1; -; Genomic_DNA.
DR   RefSeq; WP_011635611.1; NC_008345.1.
DR   AlphaFoldDB; Q089T3; -.
DR   SMR; Q089T3; -.
DR   STRING; 318167.Sfri_0119; -.
DR   EnsemblBacteria; ABI69982; ABI69982; Sfri_0119.
DR   KEGG; sfr:Sfri_0119; -.
DR   eggNOG; COG2603; Bacteria.
DR   HOGENOM; CLU_043456_1_0_6; -.
DR   OMA; RPLVYCW; -.
DR   OrthoDB; 1052499at2; -.
DR   Proteomes; UP000000684; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR017582; SelU.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   Reference proteome; Selenium; Transferase.
FT   CHAIN           1..366
FT                   /note="tRNA 2-selenouridine synthase"
FT                   /id="PRO_0000292710"
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   366 AA;  41556 MW;  3C365203FF76AB68 CRC64;
     MSEVIPSSEY GRLLLENRPL IDVRAPIEFT KGAFGHSINL PLMQDGEREK VGTCYKKRGQ
     EAAIALGHEL VKGKVKQQRI DAWLAQLSQH PDSYLYCFRG GLRSKLSQQW IKESGMDIPY
     IEGGYKAIRS FLINTIEQAP SQSKVLILSG ITGSGKTEVI HQRDESVDLE GLANHKGSSF
     GKNIDPQPSQ INFENNLAVA LLKHQQQQHN HLLLEDESML IGRSALPKHF YSAMQQADII
     VLDEPLDARL PRLLNDYVEQ KLTDYVSGLG EQAGFDAFKA YLAQSLLGIR KRLGGKQHQE
     LQDLVDNALN VQQSQNDTSK HLDWINLLLD IYYDPMYLYQ LEKKQDRVIF QGDRQAIHQW
     LDKHKS
 
 
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