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Database: UniProt
Entry: I0R1W5_9MICO
LinkDB: I0R1W5_9MICO
Original site: I0R1W5_9MICO 
ID   I0R1W5_9MICO            Unreviewed;       361 AA.
AC   I0R1W5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Sulfurtransferase {ECO:0000256|RuleBase:RU000507};
GN   ORFNames=IMCC13023_03300 {ECO:0000313|EMBL:EIC91851.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91851.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT   member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
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:EIC91851.1}.
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DR   EMBL; AJKR01000002; EIC91851.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0R1W5; -.
DR   STRING; 1081644.IMCC13023_03300; -.
DR   PATRIC; fig|1081644.3.peg.334; -.
DR   eggNOG; COG2897; Bacteria.
DR   Proteomes; UP000054510; 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:SF1; THIOSULFATE SULFURTRANSFERASE SSEA-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:UP000054510};
KW   Transferase {ECO:0000256|RuleBase:RU000507}.
FT   DOMAIN          103..210
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          249..357
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   361 AA;  38679 MW;  AF807CF4AD90A83E CRC64;
     MNVAVCYSLT LTLRQQTLAL IYLIQTTNRG TGISMIKGIR KFSTIGAASL LAVSLVGCAE
     AGSGPDSSGN KVEAEAALFD PGVTTVTTTE GLVSTDWLEQ NLDDPDLVVL QIANEEGLYE
     RGHIPEAQKL DWYSGLTGGE SRGIIDAASF QAITSSLGIN QDSKVIVYGE THQLFATWAV
     WVLKIYGFNN VRLLDGGWSK WQAEGKQVSL AQPTVELGDF VPTEANLELR AFIEEVVATA
     SAGPDTNSII VDNRSLESYV GEETSGAKFD GHVASAENLF SFALFNEDVS YLQPAEIAAA
     YQAIGATADK EVILYCGTGL LASASWFALT QILGYEDVKN YDGSWTEYGN AENVPIENAV
     S
//
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