THTR_DEIRA
ID THTR_DEIRA Reviewed; 286 AA.
AC Q9RXT9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Thiosulfate sulfurtransferase;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese-like protein;
GN OrderedLocusNames=DR_0217;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-14.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT "Protein recycling is a major component of post-irradiation recovery in
RT Deinococcus radiodurans strain R1.";
RL Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33542; EC=2.8.1.1;
CC Evidence={ECO:0000250|UniProtKB:P52197};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
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DR EMBL; AE000513; AAF09800.1; -; Genomic_DNA.
DR PIR; D75547; D75547.
DR RefSeq; NP_293941.1; NC_001263.1.
DR RefSeq; WP_010886863.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RXT9; -.
DR SMR; Q9RXT9; -.
DR STRING; 243230.DR_0217; -.
DR EnsemblBacteria; AAF09800; AAF09800; DR_0217.
DR KEGG; dra:DR_0217; -.
DR PATRIC; fig|243230.17.peg.382; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_1_3_0; -.
DR InParanoid; Q9RXT9; -.
DR OMA; LLDVRWQ; -.
DR OrthoDB; 1385159at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..286
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000139408"
FT DOMAIN 19..126
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000305"
FT DOMAIN 160..280
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000305"
FT ACT_SITE 239
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 32270 MW; 6C90D21377E11FD9 CRC64;
MDYAKDVLVS TEWAAQNLQT PGVRFIEVDE DILLYETGHL PGAVKLDWQT DLWHPVERDF
IEPQQVSELL GKLGIKADDT IVLYGDKSNW WASYAYWFLT YSGVSNLKIM NGGRQKWVAE
GREMTTEAPT VTATTYPALQ RDESLRAYRD EVRAHLESVN NGQGAMVDVR SPDEFSGKVT
HMPNYPQEGV LRGGHIPGAR NIPWAKATNE DGTFKSADEL KALYEGEGVT ADKDVIAYCR
IAERSSHSWF VLRELLGYPK VRNYDGSWTE WGNGVGLPIE KTYSEE
