ID THTR2_MYCBO Reviewed; 320 AA.
AC Q7TX80;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 60.
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; BX248344; CAD96831.1; -; 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; WSKAAND; -.
DR ProtClustDB; CLSK824808; -.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
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: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; Cytochrome_P450; 1.
DR SUPFAM; SSF52821; Rhodanese-like; 2.
DR PROSITE; PS00380; RHODANESE_1; FALSE_NEG.
DR PROSITE; PS00683; RHODANESE_2; FALSE_NEG.
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
//
