SELU_BORPD
ID SELU_BORPD Reviewed; 374 AA.
AC A9I3Z9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, 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=Bpet3887;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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; AM902716; CAP44233.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I3Z9; -.
DR SMR; A9I3Z9; -.
DR STRING; 94624.Bpet3887; -.
DR EnsemblBacteria; CAP44233; CAP44233; Bpet3887.
DR KEGG; bpt:Bpet3887; -.
DR eggNOG; COG2603; Bacteria.
DR OMA; RPLVYCW; -.
DR Proteomes; UP000001225; 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..374
FT /note="tRNA 2-selenouridine synthase"
FT /id="PRO_1000186063"
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 374 AA; 42114 MW; 659BD465A4C2FA52 CRC64;
MRADTNNYRE LFLRDVPMLD TRAPTEFSKG AFPGAVNLPL MDDAERQQVG LCYKQRGQDA
AIALGHQLVS GPIKARRVAA WADFARAHPD GYLYCFRGGL RSQISQAWLK NEAGIEYPRV
IGGYKAMRGF LLQTIDDAVA QCGFVVLGGM TGTGKTDLLR QLDNSLDLEH HAHHRGSSFG
KHAVGQPTQI DFDNRLAIDI LKKRAAGHDR FVLEDESQAI GACSLPFELY RGMQEYPVVW
LEDTTENRVN RILRDYVIDL CAEFVDVHGP EQGFDRFAER LRQSLDNISR RLGGERHRQL
AGVMDAALAE QQRSGRVDAH RAWIAALLAQ YYDPMYAYQR QRKSQRIVFA GDHQSVLQYL
RDPPAVGRAL KGFP
