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Database: UniProt
Entry: A0A212TWB3_9ACTN
LinkDB: A0A212TWB3_9ACTN
Original site: A0A212TWB3_9ACTN 
ID   A0A212TWB3_9ACTN        Unreviewed;       281 AA.
AC   A0A212TWB3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Sulfurtransferase {ECO:0000256|RuleBase:RU000507};
GN   ORFNames=SAMN06272741_4192 {ECO:0000313|EMBL:SNC70303.1};
OS   Streptomyces sp. 2114.4.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938836 {ECO:0000313|EMBL:SNC70303.1, ECO:0000313|Proteomes:UP000198141};
RN   [1] {ECO:0000313|Proteomes:UP000198141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2114.4 {ECO:0000313|Proteomes:UP000198141};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC       thiosulfate. {ECO:0000256|ARBA:ARBA00037045}.
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:0000256|ARBA:ARBA00000653};
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DR   EMBL; FYEY01000001; SNC70303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212TWB3; -.
DR   OrthoDB; 9781034at2; -.
DR   Proteomes; UP000198141; Unassembled WGS sequence.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd01448; TST_Repeat_1; 1.
DR   CDD; cd01449; TST_Repeat_2; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR   PANTHER; PTHR43855; THIOSULFATE SULFURTRANSFERASE; 1.
DR   PANTHER; PTHR43855:SF2; THIOSULFATE SULFURTRANSFERASE-RELATED; 1.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR   PROSITE; PS00683; RHODANESE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:SNC70303.1};
KW   Transferase {ECO:0000256|RuleBase:RU000507, ECO:0000313|EMBL:SNC70303.1}.
FT   DOMAIN          18..125
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          156..276
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          182..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31619 MW;  BCCFDD15CEA83675 CRC64;
     MSRSDVLVDA DWVEAHLEDP KVVLVEVDED TSAYDKNHIK NAVRIDWKQD LQDPVRRDFV
     DQEGFEKLLS AKGIANDDTV VLYGGNNNWF ASYAYWYFKL YGHDSVKLLD GGRKKWELDS
     RDLVDGSEVP QRPATDYKAK AQNTAIRAFR DDVVAAIDNL NLVDVRSPDE FSGKLLAPAH
     LPQEQSQRPG HVPSARNIPW SKNANDDGTF KSDDELKALY EGESVDLAKD TIAYCRIGER
     SALTWFVLHE LLGQTNVKNY DGSWTEYGSL VGVPIELGAN K
//
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