TSDA_THIK1
ID TSDA_THIK1 Reviewed; 314 AA.
AC D5WYQ5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Thiosulfate dehydrogenase;
DE EC=1.8.2.2;
DE AltName: Full=Tetrathionate synthase;
DE Flags: Precursor;
GN Name=tsdA; OrderedLocusNames=Tint_2892;
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=22779704; DOI=10.1111/j.1462-2920.2012.02820.x;
RA Denkmann K., Grein F., Zigann R., Siemen A., Bergmann J., van Helmont S.,
RA Nicolai A., Pereira I.A., Dahl C.;
RT "Thiosulfate dehydrogenase: a widespread unusual acidophilic c-type
RT cytochrome.";
RL Environ. Microbiol. 14:2673-2688(2012).
CC -!- FUNCTION: Catalyzes the oxidation of 2 molecules of thiosulfate to
CC tetrathionate, using TsdB as an electron acceptor.
CC {ECO:0000269|PubMed:22779704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + 2 thiosulfate = 2 Fe(II)-
CC [cytochrome c] + 2 H(+) + tetrathionate; Xref=Rhea:RHEA:20549,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15226,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:33542; EC=1.8.2.2;
CC Evidence={ECO:0000269|PubMed:22779704};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=121000 umol/min/mg enzyme (at pH 3.0)
CC {ECO:0000269|PubMed:22779704};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:22779704}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:22779704}.
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DR EMBL; CP002021; ADG32232.1; -; Genomic_DNA.
DR AlphaFoldDB; D5WYQ5; -.
DR SMR; D5WYQ5; -.
DR STRING; 75379.Tint_2892; -.
DR EnsemblBacteria; ADG32232; ADG32232; Tint_2892.
DR KEGG; tin:Tint_2892; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_058582_1_0_4; -.
DR OMA; IYENMPF; -.
DR BioCyc; TINT75379:TINT_RS14495-MON; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050338; F:thiosulfate dehydrogenase activity; IDA:UniProtKB.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..314
FT /note="Thiosulfate dehydrogenase"
FT /id="PRO_5000590631"
FT DOMAIN 58..192
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 185..270
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 90
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 94
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 198
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 201
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 202
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 314 AA; 34039 MW; C23925AA2B65E4E6 CRC64;
MTRKQTPMTL ALCALGLFAA SAASALAADA PMAPPKSEIN AAVGTGAKFT PPPESAIPDD
DFGKMVKLGR DIMLDTPKYA KDYVGNTLSC VNCHTDAGRM AGSAPLWAAY VSYPAYRGKN
KKVNTFEERL QGCFKFSQNG KAPPLGSKTL VALESYSYWL SKGLPVDEKV AGRGYPNLPE
PQQAPDYVRG QKVYEAKCIL CHAANGEGQY VNGETVFPPL WGPKSFNWGA GMGSYKNAAK
FIYANMPYGM SYSLSPQEAW DVAYFMDAQE RPQDPRWQGS VAATRAKFHD SKFSLYGTKV
NGKLLGDIGA PKPR
