TSDA_ALLVD
ID TSDA_ALLVD Reviewed; 270 AA.
AC D3RVD4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Thiosulfate dehydrogenase;
DE EC=1.8.2.2;
DE AltName: Full=Tetrathionate synthase;
DE Flags: Precursor;
GN Name=tsdA; OrderedLocusNames=Alvin_0091;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [2]
RP PROTEIN SEQUENCE OF 28-72, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=16995898; DOI=10.1111/j.1365-2958.2006.05408.x;
RA Hensen D., Sperling D., Trueper H.G., Brune D.C., Dahl C.;
RT "Thiosulphate oxidation in the phototrophic sulphur bacterium
RT Allochromatium vinosum.";
RL Mol. Microbiol. 62:794-810(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-123.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
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).
RN [4]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Catalyzes the oxidation of 2 molecules of thiosulfate to
CC tetrathionate. {ECO:0000269|PubMed:16995898,
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; Evidence={ECO:0000269|PubMed:16995898,
CC ECO:0000269|PubMed:22779704};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=30000 umol/min/mg enzyme (with 1 mM ferricyanide)
CC {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704};
CC pH dependence:
CC Optimum pH is 4.2. {ECO:0000269|PubMed:16995898,
CC ECO:0000269|PubMed:22779704};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16995898,
CC ECO:0000269|PubMed:22779704}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16995898}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC {ECO:0000269|PubMed:22779704}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to produce tetrathionate from
CC thiosulfate. {ECO:0000269|PubMed:22779704}.
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DR EMBL; CP001896; ADC61061.1; -; Genomic_DNA.
DR RefSeq; WP_012969337.1; NC_013851.1.
DR PDB; 4V2K; X-ray; 1.29 A; A=28-270.
DR PDB; 4WQ7; X-ray; 1.98 A; A=29-270.
DR PDB; 4WQ8; X-ray; 1.40 A; A=29-270.
DR PDB; 4WQ9; X-ray; 1.47 A; A=29-270.
DR PDB; 4WQA; X-ray; 1.64 A; A=29-270.
DR PDB; 4WQB; X-ray; 1.50 A; A=29-270.
DR PDB; 4WQC; X-ray; 1.56 A; A=29-270.
DR PDB; 4WQD; X-ray; 1.22 A; A=29-270.
DR PDB; 4WQE; X-ray; 1.40 A; A=29-270.
DR PDBsum; 4V2K; -.
DR PDBsum; 4WQ7; -.
DR PDBsum; 4WQ8; -.
DR PDBsum; 4WQ9; -.
DR PDBsum; 4WQA; -.
DR PDBsum; 4WQB; -.
DR PDBsum; 4WQC; -.
DR PDBsum; 4WQD; -.
DR PDBsum; 4WQE; -.
DR AlphaFoldDB; D3RVD4; -.
DR SMR; D3RVD4; -.
DR STRING; 572477.Alvin_0091; -.
DR EnsemblBacteria; ADC61061; ADC61061; Alvin_0091.
DR KEGG; alv:Alvin_0091; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_058582_2_0_6; -.
DR OMA; IYENMPF; -.
DR OrthoDB; 1297285at2; -.
DR BioCyc; MetaCyc:MON-13248; -.
DR BRENDA; 1.8.2.2; 257.
DR SABIO-RK; D3RVD4; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IMP:CACAO.
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; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:16995898"
FT CHAIN 28..270
FT /note="Thiosulfate dehydrogenase"
FT /id="PRO_5000576211"
FT DOMAIN 44..158
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 174..260
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 76
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 79
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 80
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 187
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 190
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 191
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"
FT MUTAGEN 123
FT /note="C->G: Loss of function."
FT /evidence="ECO:0000269|PubMed:22779704"
FT CONFLICT 50
FT /note="E -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="P -> PR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:4V2K"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4V2K"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4V2K"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:4V2K"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:4V2K"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:4V2K"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4V2K"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:4V2K"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4V2K"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:4V2K"
SQ SEQUENCE 270 AA; 28563 MW; BC0E598FD13D774B CRC64;
MRGDVRVHTA SPIAAAWLLA VGLVAHAEEP PTVALTVPAA ALLPDGALGE SIVRGRRYLS
DTPAQLPDFV GNGLACRHCH PGRDGEVGTE ANAAPFVGVV GRFPQYSARH GRLITLEQRI
GDCFERSLNG RALALDHPAL IDMLAYMSWL SQGVPVGAVV AGHGIPTLTL EREPDGVHGE
ALYQARCLAC HGADGSGTLD ADGRYLFPPL WGPRSFNTGA GMNRQATAAG FIKHKMPLGA
DDSLSDEEAW DVAGFVLTHP RPLFQEPTGD
