SELU_PSEE4
ID SELU_PSEE4 Reviewed; 371 AA.
AC Q1IEL0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=PSEEN0990;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(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; CT573326; CAK13895.1; -; Genomic_DNA.
DR RefSeq; WP_011532320.1; NC_008027.1.
DR AlphaFoldDB; Q1IEL0; -.
DR SMR; Q1IEL0; -.
DR STRING; 384676.PSEEN0990; -.
DR PRIDE; Q1IEL0; -.
DR EnsemblBacteria; CAK13895; CAK13895; PSEEN0990.
DR KEGG; pen:PSEEN0990; -.
DR eggNOG; COG2603; Bacteria.
DR HOGENOM; CLU_043456_1_0_6; -.
DR OMA; RPLVYCW; -.
DR OrthoDB; 1052499at2; -.
DR Proteomes; UP000000658; 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 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..371
FT /note="tRNA 2-selenouridine synthase"
FT /id="PRO_0000292704"
FT DOMAIN 12..135
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 371 AA; 41904 MW; 9D03981DCFFF2896 CRC64;
MRPDCTDFNT LFLDDVPMMD MRAPIEFTKG AFPGVVNLPL MNDQERQKVG TCFKQQGQSA
AIALGHQLVN GALKQQRLEA WAAFAQAHPD GYLYCFRGGL RSQIVQGWLK EAGIQYPKVV
GGYKAMRTFL LDTTQQAVEQ CDFVLLGGLT GTGKTDVLQQ LDNVLDLEGH ANHRGSSFGK
RATAQPAQID FENGLAIDML KKRARGIGQF VLEDEGRIVG SCTVPLGLYQ GMQRYPLVWL
EDAFDNRVER ILRDYVTNLC AEFVAVHGEE DGRRLFAERM RQSMANIYKR LGGERFQRLS
ELLGQALDEQ LRSGDVSLHR GWIEGLLKEY YDPMYAYQRE AKAGRIEFAG DGVEVREYLK
ARARRQHRVD L
