TSDA_PSEU5
ID TSDA_PSEU5 Reviewed; 307 AA.
AC A4VND8;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Thiosulfate dehydrogenase;
DE EC=1.8.2.2;
DE AltName: Full=Tetrathionate synthase;
DE Flags: Precursor;
GN Name=tsdA; OrderedLocusNames=PST_2843;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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=31000 umol/min/mg enzyme (at pH 4.2)
CC {ECO:0000269|PubMed:22779704};
CC Temperature dependence:
CC Optimum temperature is 20 degrees Celsius.
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; CP000304; ABP80489.1; -; Genomic_DNA.
DR RefSeq; WP_011913946.1; NC_009434.1.
DR AlphaFoldDB; A4VND8; -.
DR SMR; A4VND8; -.
DR STRING; 379731.PST_2843; -.
DR EnsemblBacteria; ABP80489; ABP80489; PST_2843.
DR KEGG; psa:PST_2843; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_058582_1_0_6; -.
DR OMA; IYENMPF; -.
DR Proteomes; UP000000233; Chromosome.
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; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..307
FT /note="Thiosulfate dehydrogenase"
FT /id="PRO_0000430263"
FT DOMAIN 59..156
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 180..265
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 85
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 88
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 89
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 193
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 196
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 197
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 307 AA; 33116 MW; 7E8349FABD883358 CRC64;
MNTQLLVTLL AMSIGGVALA AEIKMDDQSQ LTQKAGKGAG ESYFQPPQEK DLPANAYGEL
VQQGRAIFVD TQKYAAEYVG NGMNCTNCHL EQGRKANSAP LWGAYPMYPA YRKKNDKVNS
YAERVQGCFQ FSMNGTPPAA DSHVINALTA YSYWLSTGAP TGQELPGRAY PEVPQPQGGF
DIAKGKQIYA EQCAVCHGDD GQGQKAGGGY VFPPLWGKDS FNWGAGMHRI NTAAAFIKES
MPLGKGGSLS DADAWHVAAY MNSHERPQDP RLIEGSVEKT RLKYHANDGV NLYGQQVDGA
LLGQGVK
