(data stored in ACNUC10821 zone)

SWISSPROT: C8U2I5_ECO10

ID   C8U2I5_ECO10            Unreviewed;       364 AA.
AC   C8U2I5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=tRNA 2-selenouridine/geranyl-2-thiouridine synthase {ECO:0000256|HAMAP-Rule:MF_01622, ECO:0000256|SAAS:SAAS01064493};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01622, ECO:0000256|SAAS:SAAS01064486};
DE            EC=2.9.1.- {ECO:0000256|HAMAP-Rule:MF_01622, ECO:0000256|SAAS:SAAS00356069};
GN   Name=ybbB {ECO:0000313|EMBL:BAI29343.1};
GN   Synonyms=selU {ECO:0000256|HAMAP-Rule:MF_01622};
GN   OrderedLocusNames=ECO103_0476 {ECO:0000313|EMBL:BAI29343.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29343.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29343.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|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:0000256|HAMAP-Rule:MF_01622,
CC         ECO:0000256|SAAS:SAAS01120034};
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:0000256|HAMAP-Rule:MF_01622,
CC         ECO:0000256|SAAS:SAAS01120033};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01622,
CC       ECO:0000256|SAAS:SAAS00356061}.
CC   -!- SIMILARITY: Belongs to the SelU family. {ECO:0000256|HAMAP-
CC       Rule:MF_01622, ECO:0000256|SAAS:SAAS01064488}.
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DR   EMBL; AP010958; BAI29343.1; -; Genomic_DNA.
DR   RefSeq; WP_001158001.1; NC_013353.1.
DR   EnsemblBacteria; BAI29343; BAI29343; ECO103_0476.
DR   KEGG; eoh:ECO103_0476; -.
DR   HOGENOM; HOG000260000; -.
DR   KO; K06917; -.
DR   OMA; RPLVYCW; -.
DR   BioCyc; ECOL585395:ECO103_RS02490-MONOMER; -.
DR   Proteomes; UP000000959; 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; 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; SSF52821; SSF52821; 1.
DR   TIGRFAMs; TIGR03167; tRNA_sel_U_synt; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2I5.
DR   SWISS-2DPAGE; C8U2I5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Selenium {ECO:0000256|HAMAP-Rule:MF_01622,
KW   ECO:0000256|SAAS:SAAS00433829};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01622,
KW   ECO:0000256|SAAS:SAAS00433820}.
FT   DOMAIN       14    137       Rhodanese. {ECO:0000259|PROSITE:PS50206}.
FT   ACT_SITE     97     97       S-selanylcysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01622}.
SQ   SEQUENCE   364 AA;  41130 MW;  B1447A1C972DD855 CRC64;
     MQERHTEQDY RALLIADTPI IDVRAPIEFE QGAMPAAINL PLMNNDERAA VGTCYKQQGS
     DAALALGHKL VAGEIRQQRM DAWRAACLQN PQGILCCARG GQRSHIVQSW LYAAGIDYPL
     VEGGYKALRQ TAIQATIELA QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG
     RTLQPQLSQA SFENLLAAEM LKTDARQDLR LWVLEDESRM IGSNHLPECL RERMTQAAIA
     VVEDPFEIRL ERLNEEYFLR MHHDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE
     LAAQLDTALT TQLTTGSTDG HLAWLVPLLK EYYDPMYRYQ LEKKAEKVVF RGEWAEVAEW
     VKAR
//

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