ID W0DV27_9GAMM Unreviewed; 367 AA.
AC W0DV27;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=tRNA 2-selenouridine synthase {ECO:0000256|HAMAP-Rule:MF_01622};
DE EC=2.9.1.3 {ECO:0000256|HAMAP-Rule:MF_01622};
GN Name=selU {ECO:0000256|HAMAP-Rule:MF_01622};
GN ORFNames=THIAE_02020 {ECO:0000313|EMBL:AHF00706.1};
OS Thiomicrospira aerophila AL3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF00706.1, ECO:0000313|Proteomes:UP000005380};
RN [1] {ECO:0000313|EMBL:AHF00706.1, ECO:0000313|Proteomes:UP000005380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380};
RG DOE Joint Genome Institute;
RA Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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:0000256|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:0000256|HAMAP-
CC 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01622};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01622}.
CC -!- SIMILARITY: Belongs to the SelU family. {ECO:0000256|HAMAP-
CC Rule:MF_01622}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP007030; AHF00706.1; -; Genomic_DNA.
DR RefSeq; WP_006459825.1; NZ_CP007030.1.
DR AlphaFoldDB; W0DV27; -.
DR STRING; 717772.THIAE_02020; -.
DR KEGG; tao:THIAE_02020; -.
DR eggNOG; COG2603; Bacteria.
DR HOGENOM; CLU_043456_1_0_6; -.
DR InParanoid; W0DV27; -.
DR OrthoDB; 9808735at2; -.
DR Proteomes; UP000005380; 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; Rhodanese-like domain; 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 NCBIfam; TIGR03167; tRNA_sel_U_synt; 1.
DR PANTHER; PTHR30401; TRNA 2-SELENOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR30401:SF0; TRNA 2-SELENOURIDINE SYNTHASE; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_01622};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01622}.
FT DOMAIN 15..138
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 98
FT /note="S-selanylcysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01622"
SQ SEQUENCE 367 AA; 40822 MW; 28BBEAB959F71892 CRC64;
MSRELPTVDN YAAIALAQTP LLDVRAPVEF ERGAIPQATN LPLMNDDERH QVGLCYKQRG
QQQAIALGHQ LVQGDLRAER LASWQAFFSQ HPNGLLYCFR GGLRSRTSQQ WLADAGVEVA
RIAGGYKAFR QYLIDTLDQT AAALEQGALA SWILAGRTGS GKTALLQHLP GAVDLEGLAQ
HRGSSFGGRA WSQPSQIDFE NRLAYRLIEL NAQPIRQRVF EDEARNIGSV HLSPPLFNAI
KAGKRIVLDV PFDTRCQHIL QEYVIEGQLE FGGLNAWMAH MQARFARIAK RLGGVGYTKL
SHAFEQACIE QQATGDFGAH ISWIAPLLQD YYDPMYDYQL KRHSQPVIMR GGAQDVSAFM
QHISSVN
//
