ID D9VQ80_9ACTN Unreviewed; 281 AA.
AC D9VQ80;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Sulfurtransferase {ECO:0000256|RuleBase:RU000507};
GN ORFNames=SSNG_03788 {ECO:0000313|EMBL:EFL16536.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL16536.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL16536.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL16536.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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; GG657750; EFL16536.1; -; Genomic_DNA.
DR RefSeq; WP_007265475.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VQ80; -.
DR STRING; 253839.SSNG_03788; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_1_3_11; -.
DR Proteomes; UP000005763; 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 Transferase {ECO:0000256|RuleBase:RU000507, ECO:0000313|EMBL:EFL16536.1}.
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..207
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; 31649 MW; D9382098CDE422FA CRC64;
MSRSDVLVDA DWVEAHLNDA NVVIVEVDED TSAYDKNHIT NAVRIDWKQD LQDPVRRDFV
DQEGFEKLLS AKGISNDDTV VLYGGNNNWF ASYAYWYFKL YGHQDVKLLD GGRKKWELDS
RDLVDGKDVP NRPATEYKAK AQDTSIRAFR DDVVAAIGSL NLVDVRSPDE FSGKLLAPAH
LPQEQSQRPG HVPSARNIPW SKNANDDGTF KSDEELTALY EAEQVDLAKD TIAYCRIGER
SALTWFVLHE LLGQENVKNY DGSWTEYGSL VGVPIELGPN K
//