TSDA_PSYA2
ID TSDA_PSYA2 Reviewed; 327 AA.
AC Q4FQB7;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Thiosulfate dehydrogenase;
DE EC=1.8.2.2;
DE AltName: Full=Tetrathionate synthase;
DE Flags: Precursor;
GN Name=tsdA; OrderedLocusNames=Psyc_1943;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
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. {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=33.4 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:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Binds 2 heme c groups covalently per subunit. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells are unable to produce tetrathionate from
CC thiosulfate. {ECO:0000269|PubMed:22779704}.
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DR EMBL; CP000082; AAZ19791.1; -; Genomic_DNA.
DR RefSeq; WP_011281200.1; NC_007204.1.
DR AlphaFoldDB; Q4FQB7; -.
DR SMR; Q4FQB7; -.
DR STRING; 259536.Psyc_1943; -.
DR PRIDE; Q4FQB7; -.
DR EnsemblBacteria; AAZ19791; AAZ19791; Psyc_1943.
DR KEGG; par:Psyc_1943; -.
DR eggNOG; COG3258; Bacteria.
DR HOGENOM; CLU_058582_2_0_6; -.
DR OMA; IYENMPF; -.
DR OrthoDB; 1297285at2; -.
DR Proteomes; UP000000546; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..327
FT /note="Thiosulfate dehydrogenase"
FT /id="PRO_0000430264"
FT DOMAIN 99..196
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 219..305
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 66..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
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 128
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 129
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 232
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 235
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 236
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 327 AA; 35260 MW; A65B1EA961DFF3B3 CRC64;
MKIIPYRKRS VLIATIFAIS AVGITGCSDN TETKAVERVE EAAALARVKD LEARAEALKS
NMPAANDMTA TAGGTDTASG KPTIKMPDES TIPDDEFGAA VRRGLQISNH TYKELPNNVG
NQLNCTSCHL GNGSEAYAAP WNNTPSVYPN YSKRTGRINT IQERINGCFE RSLNGKALDL
NSDDMNAMVS YMSWLSQDMP FGVSPEGSGF VKVDKTLEPN TDNGKKLFAE KCSVCHGATG
EGQYNDDGTY VYPAIAGDKS FNDGAGMART YTAASFIKGK MPFGQGGSLS DQEAVDIASY
FTHLPRPIKA NKDKDWPNGD APKDVRR
