(data stored in ACNUC7421 zone)

SWISSPROT: SELU_ECODH

ID   SELU_ECODH              Reviewed;         364 AA.
AC   B1XFT8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 59.
DE   RecName: Full=tRNA 2-selenouridine synthase {ECO:0000255|HAMAP-Rule:MF_01622};
DE            EC=2.9.1.- {ECO:0000255|HAMAP-Rule:MF_01622};
DE   AltName: Full=Selenophosphate-dependent tRNA 2-selenouridine synthase {ECO:0000255|HAMAP-Rule:MF_01622};
GN   Name=selU {ECO:0000255|HAMAP-Rule:MF_01622};
GN   OrderedLocusNames=ECDH10B_0459;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the transfer of selenium from selenophosphate
CC       for conversion of 2-thiouridine to 2-selenouridine at the wobble
CC       position in tRNA. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- CATALYTIC ACTIVITY: 5-methylaminomethyl-2-thiouridine +
CC       selenophosphate = 5-methylaminomethyl-2-selenouridine + phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01622}.
CC   -!- SIMILARITY: Belongs to the 2-selenouridine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01622}.
DR   EMBL; CP000948; ACB01628.1; -; Genomic_DNA.
DR   RefSeq; WP_001157938.1; NC_010473.1.
DR   ProteinModelPortal; B1XFT8; -.
DR   SMR; B1XFT8; -.
DR   EnsemblBacteria; ACB01628; ACB01628; ECDH10B_0459.
DR   KEGG; ecd:ECDH10B_0459; -.
DR   eggNOG; ENOG4105CR7; Bacteria.
DR   eggNOG; COG2603; LUCA.
DR   HOGENOM; HOG000260000; -.
DR   KO; K06917; -.
DR   OMA; YCWRGGM; -.
DR   GO; GO:0043828; F:tRNA 2-selenouridine synthase activity; IEA:InterPro.
DR   GO; GO:0070329; P:tRNA seleno-modification; IEA:InterPro.
DR   Gene3D; 3.40.250.10; -; 1.
DR   HAMAP; MF_01622; tRNA_sel_U_synth; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR017582; tRNA_2-selenouridine_synthase.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   TIGRFAMs; TIGR03167; tRNA_sel_U_synt; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XFT8.
DR   SWISS-2DPAGE; B1XFT8.
KW   Selenium; Transferase.
FT   CHAIN         1    364       tRNA 2-selenouridine synthase.
FT                                /FTId=PRO_1000186071.
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;  41111 MW;  8C0F244BA86B6C4A CRC64;
     MQERHTEQDY RALLIADTPI IDVRAPIEFE HGAMPAAINL PLMNNDERAA VGTCYKQQGS
     DAALALGHKL VAGEIRQQRM DAWRAACLQN PQGILCCARG GQRSHIVQSW LHAAGIDYPL
     VEGGYKALRQ TAIQATIELA QKPIVLIGGC TGSGKTLLVQ QQPNGVDLEG LARHRGSAFG
     RTLQPQLSQA SFENLLAAEM LKTDARQNLR LWVLEDESRM IGSNHLPECL RERMTQAAIA
     VVEDPFEIRL ERLNEEYFLR MHHDFTHAYG DEQGWQEYCE YLHHGLSAIK RRLGLQRYNE
     LAARLDAALT TQLTTGSTDG HLAWLVPLLE EYYDPMYRYQ LEKKAEKVVF RGEWAEVAEW
     VKAR
//

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