(data stored in ACNUC7421 zone)

SWISSPROT: SELU_SHISS

ID   SELU_SHISS              Reviewed;         364 AA.
AC   Q3Z4Q0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=tRNA 2-selenouridine/geranyl-2-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.9.1.- {ECO:0000255|HAMAP-Rule:MF_01622};
GN   Name=selU {ECO:0000255|HAMAP-Rule:MF_01622};
GN   OrderedLocusNames=SSON_0486;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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 selenation and geranylation of 2-
CC       thiouridine, forming 5-methylaminomethyl-2-selenouridine
CC       (mnm5Se2U) and geranylated 5-methylaminomethyl-2-thiouridine
CC       (mnm5ges2U), respectively. The two reactions may occur
CC       independently or in a linear manner, where S-geranyl-2-thiouridine
CC       is an intermediate of the conversion of 2-thiouridine to 2-
CC       selenouridine. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) +
CC         selenophosphate = 5-methylaminomethyl-2-selenouridine(34) in
CC         tRNA + thiophosphate; Xref=Rhea:RHEA:42716, Rhea:RHEA-
CC         COMP:10195, Rhea:RHEA-COMP:10196, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:74455, ChEBI:CHEBI:74752,
CC         ChEBI:CHEBI:82743; 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   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- SIMILARITY: Belongs to the SelU family. {ECO:0000255|HAMAP-
CC       Rule:MF_01622}.
DR   EMBL; CP000038; AAZ87262.1; -; Genomic_DNA.
DR   SMR; Q3Z4Q0; -.
DR   EnsemblBacteria; AAZ87262; AAZ87262; SSON_0486.
DR   KEGG; ssn:SSON_0486; -.
DR   HOGENOM; HOG000260000; -.
DR   KO; K06917; -.
DR   OMA; RPLVYCW; -.
DR   BioCyc; SSON300269:G1GL2-558-MONOMER; -.
DR   Proteomes; UP000002529; 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:InterPro.
DR   GO; GO:0070329; P:tRNA seleno-modification; IEA:InterPro.
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; tRNA_2-selenouridine_synthase.
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;
DR   PRODOM; Q3Z4Q0.
DR   SWISS-2DPAGE; Q3Z4Q0.
KW   Complete proteome; Selenium; Transferase.
FT   CHAIN         1    364       tRNA 2-selenouridine/geranyl-2-
FT                                thiouridine synthase.
FT                                /FTId=PRO_0000210878.
FT   DOMAIN       14    137       Rhodanese. {ECO:0000255|HAMAP-
FT                                Rule:MF_01622}.
FT   ACT_SITE     97     97       S-selanylcysteine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_01622}.
SQ   SEQUENCE   364 AA;  41160 MW;  51C776B9163772FF CRC64;
     MQERHTEQDY RALLIADTPI IDVRAPIEFE QGAMPAAINL PLMNNDERAA VGTCYKQQGS
     DAALALGHKL VAGEIRQQRM DAWRAACLQN PQGILCCARG GQRSHIVQSW LYAAGIDYPL
     VEGGYKALRQ AAIQATIELA QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG
     RTLQPQLSQA SFENLLAAEM LKTDARQDLR LWVLEDESRM IGSNHLPECL RERMTQAAIA
     VVEDPFEIRL ERLNEEYFLR MHHDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE
     LAAQLDTALT TQLTTDSTDG HLAWLVPLLK EYYDPMYRYQ LEKKAEKVVF RGEWAEVAEW
     VKTQ
//

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