SELU_PSEP1
ID SELU_PSEP1 Reviewed; 370 AA.
AC A5VYQ1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Pput_0849;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-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; CP000712; ABQ77011.1; -; Genomic_DNA.
DR RefSeq; WP_004576353.1; NC_009512.1.
DR AlphaFoldDB; A5VYQ1; -.
DR SMR; A5VYQ1; -.
DR STRING; 351746.Pput_0849; -.
DR EnsemblBacteria; ABQ77011; ABQ77011; Pput_0849.
DR KEGG; ppf:Pput_0849; -.
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 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..370
FT /note="tRNA 2-selenouridine synthase"
FT /id="PRO_1000069591"
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 370 AA; 41928 MW; 50FBDAA9ACE9A142 CRC64;
MRPDCTDFRQ LFLDDVPMMD MRAPVEFAKG AFPGVVNLPL MNDQERQKVG TCYKQQGQAA
AIALGHQLVS GTTKQARLEA WAAFAKAHPD GYLYCFRGGL RSQIVQGWLR DEAGIQYPRV
KGGYKAMRTF LLETTQQAVE QCDFVLVGGL TGTGKTDVLH QLDNVLDLEG HANHRGSSFG
KRATAQPAQI DFENQLAIDV LKKRARGIGQ FVLEDEGRIV GSCTVPLELY QGMQHYPLVW
LEDSFTNRVE RILRDYVVNL SAEFKAVHGE EDGPRLFAER MLQSMANIYK RLGGERHQRL
SEMLREALQE QQRSGAVDLH RGWIEGLLNE YYDPMYAYQR AAKAERIEFA GDAVEVREYL
KARALREPRK
