ID M3BTT9_9ACTN Unreviewed; 281 AA.
AC M3BTT9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Sulfurtransferase {ECO:0000256|RuleBase:RU000507};
GN ORFNames=H114_20090 {ECO:0000313|EMBL:EMF27329.1};
OS Streptomyces gancidicus BKS 13-15.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF27329.1, ECO:0000313|Proteomes:UP000011732};
RN [1] {ECO:0000313|EMBL:EMF27329.1, ECO:0000313|Proteomes:UP000011732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF27329.1,
RC ECO:0000313|Proteomes:UP000011732};
RX PubMed=23599292;
RA Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL Genome Announc. 1:E00150-13(2013).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMF27329.1}.
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DR EMBL; AOHP01000080; EMF27329.1; -; Genomic_DNA.
DR RefSeq; WP_006133965.1; NZ_AOHP01000080.1.
DR AlphaFoldDB; M3BTT9; -.
DR PATRIC; fig|1284664.3.peg.4035; -.
DR OrthoDB; 9781034at2; -.
DR Proteomes; UP000011732; 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 Reference proteome {ECO:0000313|Proteomes:UP000011732};
KW Transferase {ECO:0000256|RuleBase:RU000507, ECO:0000313|EMBL:EMF27329.1}.
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; 31710 MW; D7EC650D863143EA CRC64;
MARSDVLVDA DWLQEHLDDP TIAIVEVDED TSAYDKNHIK NAVRIDWTED LQDPVRRDFV
DQAGFEKLLS EKGISNDHTV VLYGGNNNWF ASYAYWYFKL YGHENVKLLD GGRKKWELDA
RELVPGDEVP ERPKTDYKAK PQDTSIRAFR DDVVKAIGAQ NLVDVRSPDE FSGKLLAPAH
LPQEQSQRPG HVPSAKNIPW SKNANDDGTF KSDDELKELY AGEDVDLAKD TIAYCRIGER
SALTWFVLHE LLGVENVKNY DGSWTEYGSL VGVPIELGSG K
//