TUSD_ECODH
ID TUSD_ECODH Reviewed; 128 AA.
AC B1X6J4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Sulfurtransferase TusD {ECO:0000255|HAMAP-Rule:MF_00390};
DE EC=2.8.1.- {ECO:0000255|HAMAP-Rule:MF_00390};
DE AltName: Full=tRNA 2-thiouridine synthesizing protein D {ECO:0000255|HAMAP-Rule:MF_00390};
GN Name=tusD {ECO:0000255|HAMAP-Rule:MF_00390};
GN OrderedLocusNames=ECDH10B_3520;
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 the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
CC -!- FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5-
CC methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
CC Accepts sulfur from TusA and transfers it in turn to TusE.
CC {ECO:0000255|HAMAP-Rule:MF_00390}.
CC -!- SUBUNIT: Heterohexamer, formed by a dimer of trimers. The hexameric
CC TusBCD complex contains 2 copies each of TusB, TusC and TusD. The
CC TusBCD complex interacts with TusE. {ECO:0000255|HAMAP-Rule:MF_00390}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00390}.
CC -!- SIMILARITY: Belongs to the DsrE/TusD family. {ECO:0000255|HAMAP-
CC Rule:MF_00390}.
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; CP000948; ACB04404.1; -; Genomic_DNA.
DR RefSeq; WP_001209680.1; NC_010473.1.
DR AlphaFoldDB; B1X6J4; -.
DR SMR; B1X6J4; -.
DR KEGG; ecd:ECDH10B_3520; -.
DR HOGENOM; CLU_132095_0_0_6; -.
DR OMA; PQDDRNI; -.
DR BioCyc; ECOL316385:ECDH10B_RS17890-MON; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1260.10; -; 1.
DR HAMAP; MF_00390; Thiourid_synth_D; 1.
DR InterPro; IPR027396; DsrEFH-like.
DR InterPro; IPR003787; Sulphur_relay_DsrE/F-like.
DR InterPro; IPR017463; Sulphur_relay_TusD/DsrE.
DR Pfam; PF02635; DrsE; 1.
DR SUPFAM; SSF75169; SSF75169; 1.
DR TIGRFAMs; TIGR03012; sulf_tusD_dsrE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Transferase; tRNA processing.
FT CHAIN 1..128
FT /note="Sulfurtransferase TusD"
FT /id="PRO_1000122860"
FT ACT_SITE 78
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00390"
SQ SEQUENCE 128 AA; 13641 MW; 87B2754849A0FEFF CRC64;
MRFAIVVTGP AYGTQQASSA FQFAQALIAD GHELSSVFFY REGVYNANQL TSPASDEFDL
VRAWQQLNAQ HGVALNICVA AALRRGVVDE TEAGRLGLAS SNLQQGFTLS GLGALAEASL
TCDRVVQF