ID D6ZEK0_SEGRD Unreviewed; 277 AA.
AC D6ZEK0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Sulfurtransferase {ECO:0000256|RuleBase:RU000507};
GN OrderedLocusNames=Srot_3052 {ECO:0000313|EMBL:ADG99476.1};
OS Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS 44985 / JCM 13578).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC Segniliparus.
OX NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG99476.1, ECO:0000313|Proteomes:UP000002247};
RN [1] {ECO:0000313|EMBL:ADG99476.1, ECO:0000313|Proteomes:UP000002247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC {ECO:0000313|Proteomes:UP000002247};
RX PubMed=21304703; DOI=10.4056/sigs.791633;
RA Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT 1076).";
RL Stand. Genomic Sci. 2:203-211(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001958; ADG99476.1; -; Genomic_DNA.
DR RefSeq; WP_013139923.1; NC_014168.1.
DR AlphaFoldDB; D6ZEK0; -.
DR STRING; 640132.Srot_3052; -.
DR KEGG; srt:Srot_3052; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_031618_1_3_11; -.
DR OrthoDB; 9781034at2; -.
DR Proteomes; UP000002247; Chromosome.
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; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW Transferase {ECO:0000256|RuleBase:RU000507, ECO:0000313|EMBL:ADG99476.1}.
FT DOMAIN 18..125
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 154..274
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 277 AA; 31050 MW; B3E8F8FC215DE06E CRC64;
MSREHVLVSA DWAAEHLNDP AVVFVEVDED TEAYEFGHLP GAVRLDWRTE LQDPVRRDFV
SKEGFEKLLS SKGIAREDTV VLYGGNNNWF AAYAYWYFTL YGHEDVRLLD GGRKKWELDG
RLLTATVPDR PTTDYKASEP DTSIRAFRDE VISAIGTANL VDVRSPDEFS GKILAPAHLP
QEQSQRRGHI PGAINVPWSK AANEDGTFKS DEELRELYTG AGLDPGKETI AYCRIGERSS
HTWFVLKELL GQDKVKNYDG SWTEYGALVG VPIELGA
//
