THT2_MYCBO
ID THT2_MYCBO Reviewed; 297 AA.
AC Q7TWT6; A0A1R3Y3P8; X2BN61;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative thiosulfate sulfurtransferase SseA;
DE EC=2.8.1.1;
GN Name=sseA; OrderedLocusNames=BQ2027_MB3311;
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 -!- 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; SIU01940.1; -; Genomic_DNA.
DR RefSeq; NP_856956.1; NC_002945.3.
DR RefSeq; WP_010950863.1; NC_002945.4.
DR AlphaFoldDB; Q7TWT6; -.
DR SMR; Q7TWT6; -.
DR EnsemblBacteria; SIU01940; SIU01940; BQ2027_MB3311.
DR PATRIC; fig|233413.5.peg.3640; -.
DR OMA; GYPRVKG; -.
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; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 3: Inferred from homology;
KW Repeat; Transferase.
FT CHAIN 1..297
FT /note="Putative thiosulfate sulfurtransferase SseA"
FT /id="PRO_0000139416"
FT DOMAIN 31..138
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 168..286
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 245
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 297 AA; 33379 MW; F6327B5F9C617532 CRC64;
MPLPADPSPT LSAYAHPERL VTADWLSAHM GAPGLAIVES DEDVLLYDVG HIPGAVKIDW
HTDLNDPRVR DYINGEQFAE LMDRKGIARD DTVVIYGDKS NWWAAYALWV FTLFGHADVR
LLNGGRDLWL AERRETTLDV PTKTCTGYPV VQRNDAPIRA FRDDVLAILD AQPLIDVRSP
EEYTGKRTHM PDYPEEGALR AGHIPTAVHI PWGKAADESG RFRSREELER LYDFINPDDQ
TVVYCRIGER SSHTWFVLTH LLGKADVRNY DGSWTEWGNA VRVPIVAGEE PGVVPVV
