ID   THTR_CORGL              Reviewed;         301 AA.
AC   P71121;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Thiosulfate sulfurtransferase;
DE            EC=2.8.1.1;
GN   Name=thtR; OrderedLocusNames=Cgl0701, cg0803;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-301.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=8772169; DOI=10.1007/s002030050359;
RA   Jaeger W., Peters-Wendisch P.G., Kalinowski J., Puehler A.;
RT   "A Corynebacterium glutamicum gene encoding a two-domain protein similar to
RT   biotin carboxylases and biotin-carboxyl-carrier proteins.";
RL   Arch. Microbiol. 166:76-82(1996).
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   -!- 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; BA000036; BAB98094.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19406.1; -; Genomic_DNA.
DR   EMBL; U35023; AAB40889.1; -; Genomic_DNA.
DR   RefSeq; NP_599933.1; NC_003450.3.
DR   RefSeq; WP_011013827.1; NC_006958.1.
DR   AlphaFoldDB; P71121; -.
DR   SMR; P71121; -.
DR   STRING; 196627.cg0803; -.
DR   KEGG; cgb:cg0803; -.
DR   KEGG; cgl:Cgl0701; -.
DR   PATRIC; fig|196627.13.peg.687; -.
DR   eggNOG; COG2897; Bacteria.
DR   HOGENOM; CLU_031618_1_3_11; -.
DR   OMA; GYPRVKG; -.
DR   Proteomes; UP000000582; Chromosome.
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   3: Inferred from homology;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..301
FT                   /note="Thiosulfate sulfurtransferase"
FT                   /id="PRO_0000139407"
FT   DOMAIN          31..138
FT                   /note="Rhodanese 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          171..289
FT                   /note="Rhodanese 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        248
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33494 MW;  AA18128019039F8C CRC64;
     MAAPFDPFPA FEEYAHPERI VSASWLSARL GSPGLKVVES NEDSLLYDIG HLPGAVRIDW
     AKDLNDPLTR DFIDGEAFAE LMNRKGIARD DTVVVYGDKS NWWAAFTLWV FELFGHSDVR
     LLNGGRDAWM AEERDTSYVV PEYPSANYPV VERVDENQRA FVAEVLGSLT QSGGMTLVDV
     RTPSEFSGLD EHGNPTSNTG VLRGGHIPGA INLDWSDAVL PNGNFRTRAE LDKLYADLNP
     ADDTVVYCQV GDRAAHTWFV LKYLLGFNNV RNYDGSWAEW GNMVRMPIET GENTKNNVSV
     S