THTR1_MYCBO
ID THTR1_MYCBO Reviewed; 277 AA.
AC P59989; A0A1R3XWI9; X2BG48;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative thiosulfate sulfurtransferase 1;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese-like protein 1;
GN Name=cysA1; OrderedLocusNames=BQ2027_MB0838C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; 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., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: May be a sulfotransferase involved in the formation of
CC thiosulfate. {ECO:0000250}.
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 -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
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DR EMBL; LT708304; SIT99437.1; -; Genomic_DNA.
DR RefSeq; NP_854496.1; NC_002945.3.
DR RefSeq; WP_003404293.1; NC_002945.4.
DR AlphaFoldDB; P59989; -.
DR SMR; P59989; -.
DR EnsemblBacteria; SIT99437; SIT99437; BQ2027_MB0838C.
DR PATRIC; fig|233413.5.peg.911; -.
DR OMA; QRPGHVP; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 3: Inferred from homology;
KW Repeat; Transferase.
FT CHAIN 1..277
FT /note="Putative thiosulfate sulfurtransferase 1"
FT /id="PRO_0000139412"
FT DOMAIN 18..125
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 154..274
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 233
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 277 AA; 31015 MW; AC37B715D99565A9 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 GHQNVKNYDG SWTEYGSLVG APIELGS
