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SELU_SALPB
ID   SELU_SALPB              Reviewed;         364 AA.
AC   A9MW55;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=SPAB_03051;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-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; CP000886; ABX68414.1; -; Genomic_DNA.
DR   RefSeq; WP_001154086.1; NC_010102.1.
DR   AlphaFoldDB; A9MW55; -.
DR   SMR; A9MW55; -.
DR   KEGG; spq:SPAB_03051; -.
DR   PATRIC; fig|1016998.12.peg.2879; -.
DR   HOGENOM; CLU_043456_1_0_6; -.
DR   OMA; RPLVYCW; -.
DR   BioCyc; SENT1016998:SPAB_RS12455-MON; -.
DR   Proteomes; UP000008556; 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   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..364
FT                   /note="tRNA 2-selenouridine synthase"
FT                   /id="PRO_1000088088"
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   364 AA;  41280 MW;  8EFB42FC0BFBB868 CRC64;
     MQDRQKAQDY RALLLADTPL IDVRAPIEFE QGAMPGAINL PLMMGDERAA VGTCYKRQGA
     DAALALGHRL VCGDIRQQRL EAWKAAYQRF PNGYLCCARG GQRSHIVQRW LKETGIDCPL
     IEGGYKALRQ TAIQATWQLA QKPILLIGGC TGSGKTQLVR QQPNGVDLEG LARHRGSSFG
     RTLKPQLSQA SFENKLAVEL LKINARQTLK RWVLEDEGRT IGANHLPECL RERMAQAPIA
     VVEDPFALRL ERLREEYFIR MHHDFTHAYG DEAGWQAYSE YLHHGLFAIR RRLGLQRFAE
     LTDTLDRALA EQLSSGSTDG HMAWLVPLLN EYYDPMYRYQ LEKKAANIVF RGPWQDVANW
     LKAQ
 
 
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