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Database: UniProt
Entry: Q7TX80
LinkDB: Q7TX80
Original site: Q7TX80 
ID   THTR2_MYCBO             Reviewed;         320 AA.
AC   Q7TX80; X2BMN5;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   11-JUN-2014, entry version 66.
DE   RecName: Full=Putative thiosulfate sulfurtransferase 2;
DE            EC=2.8.1.1;
DE   AltName: Full=Rhodanese-like protein 2;
GN   Name=cysA2; OrderedLocusNames=Mb3144;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
CC   -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC       thiosulfate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiosulfate + cyanide = sulfite + thiocyanate.
CC   -!- DOMAIN: Contains two rhodanese domains with different primary
CC       structures but with near identical secondary structure
CC       conformations suggesting a common evolutionary origin. Only the C-
CC       terminal rhodanese domain contains the catalytic cysteine residue
CC       (By similarity).
CC   -!- SIMILARITY: Contains 2 rhodanese domains.
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DR   EMBL; BX248333; CDO44414.1; -; Genomic_DNA.
DR   RefSeq; NP_856789.1; NC_002945.3.
DR   ProteinModelPortal; Q7TX80; -.
DR   STRING; 233413.Mb3144; -.
DR   EnsemblBacteria; CAD96831; CAD96831; Mb3144.
DR   GeneID; 1093127; -.
DR   KEGG; mbo:Mb3144; -.
DR   PATRIC; 18008654; VBIMycBov88188_3456.
DR   eggNOG; COG2897; -.
DR   HOGENOM; HOG000157236; -.
DR   KO; K01011; -.
DR   OMA; NAKSEFK; -.
DR   OrthoDB; EOG69WFH7; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.630.10; -; 1.
DR   Gene3D; 3.40.250.10; -; 2.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   SUPFAM; SSF52821; SSF52821; 2.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   3: Inferred from homology;
KW   Complete proteome; Repeat; Transferase.
FT   CHAIN         1    320       Putative thiosulfate sulfurtransferase 2.
FT                                /FTId=PRO_0000139413.
FT   DOMAIN       18    125       Rhodanese 1.
FT   DOMAIN      154    267       Rhodanese 2.
FT   ACT_SITE    233    233       Cysteine persulfide intermediate (By
FT                                similarity).
FT   BINDING     238    238       Substrate (By similarity).
SQ   SEQUENCE   320 AA;  35999 MW;  4D6427752BDB7B1D CRC64;
     MARCDVLVSA DWAESNLHAP KVVFVEVDED TSAYDRDHIA GAIKLDWRTD LQDPVKRDFV
     DAQQFSKLLS ERGIANEDTV ILYGGNNNWF AAYAYWYFKL YGHEKVKLLD GGRKKWELDG
     RPLSSDPVSR PVTSYTASPP DNTIRAFRDE VLAAINVKNL IDVRSPDEFS GKILAPAHLP
     QEQSQRPGHI PGAINVPWSR AANEDGTFKS DEELAKLYAD AGLDNSKETI AYCRIGERSS
     HTWFVLRELL GHQNVNIAFG YGPHACPASA YSRMCLTTFF TSLTQRFPQL QLARPFEDLE
     RRGKGLHSVG IKELLVTWPT
//
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