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SELU_PSEMY
ID   SELU_PSEMY              Reviewed;         373 AA.
AC   A4XV44;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Pmen_2454;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP85210.1; -; Genomic_DNA.
DR   RefSeq; WP_003240754.1; NC_009439.1.
DR   AlphaFoldDB; A4XV44; -.
DR   SMR; A4XV44; -.
DR   STRING; 399739.Pmen_2454; -.
DR   EnsemblBacteria; ABP85210; ABP85210; Pmen_2454.
DR   KEGG; pmy:Pmen_2454; -.
DR   PATRIC; fig|399739.8.peg.2479; -.
DR   eggNOG; COG2603; Bacteria.
DR   HOGENOM; CLU_043456_1_0_6; -.
DR   OMA; RPLVYCW; -.
DR   OrthoDB; 1052499at2; -.
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   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..373
FT                   /note="tRNA 2-selenouridine synthase"
FT                   /id="PRO_1000069590"
FT   DOMAIN          12..136
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01622"
FT   ACT_SITE        95
FT                   /note="S-selanylcysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01622"
SQ   SEQUENCE   373 AA;  41815 MW;  A145FBF187829E8F CRC64;
     MRENCTDYRD LFINDRPMMD ARAPVEFHKG AFPGVINLPL MNDIERQKVG TCYKQHGQQA
     AIELGHQLVS GRTKAERIEA WASFAKANPD GYLYCFRGGL RSQIVQQWLK SEAGIDYPRV
     IGGYKAMRGF LLETTEQAVA ECDFVLVGGM TGTGKTEVLA QLHNAVDLEA HANHRGSSFG
     KRASGQPAQI DFENALAIDL LKRRAAGQRQ FVLEDEARLI GRCSLPLPLY QGMQHYPLVW
     LEDSLGDRVE RILQAYVVEL CAEFVAVEGA EAGFAAFAAR LRESLANITR RLGGERYQRL
     AAIMDQALEE QARDGQVDTH RGWIEALLVE YYDPMYVFQR ESKAGRIEFA GEQQAVVEYL
     RQRSGHFPEA PAS
 
 
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