THTR_PSEAE
ID THTR_PSEAE Reviewed; 271 AA.
AC Q9HUK9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Thiosulfate sulfurtransferase {ECO:0000305};
DE Short=TST {ECO:0000303|PubMed:16307778};
DE EC=2.8.1.1 {ECO:0000269|PubMed:15522204};
DE AltName: Full=Rhodanese RhdA {ECO:0000303|PubMed:16307778};
DE AltName: Full=Thiosulfate:cyanide sulfurtransferase {ECO:0000303|PubMed:15522204};
GN Name=rhdA {ECO:0000303|PubMed:15522204, ECO:0000312|EMBL:AAG08341.1};
GN OrderedLocusNames=PA4956 {ECO:0000312|EMBL:AAG08341.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE
RP SITE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15522204; DOI=10.1016/j.bbrc.2004.09.214;
RA Cipollone R., Bigotti M.G., Frangipani E., Ascenzi P., Visca P.;
RT "Characterization of a rhodanese from the cyanogenic bacterium Pseudomonas
RT aeruginosa.";
RL Biochem. Biophys. Res. Commun. 325:85-90(2004).
RN [3]
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16307778; DOI=10.1016/j.chemosphere.2005.09.048;
RA Cipollone R., Ascenzi P., Frangipani E., Visca P.;
RT "Cyanide detoxification by recombinant bacterial rhodanese.";
RL Chemosphere 63:942-949(2006).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17098912; DOI=10.1128/aem.02143-06;
RA Cipollone R., Frangipani E., Tiburzi F., Imperi F., Ascenzi P., Visca P.;
RT "Involvement of Pseudomonas aeruginosa rhodanese in protection from cyanide
RT toxicity.";
RL Appl. Environ. Microbiol. 73:390-398(2007).
CC -!- FUNCTION: Catalyzes the sulfur transfer reaction from thiosulfate to
CC cyanide, thus converting cyanide to the less toxic thiocyanate
CC (PubMed:15522204). Contributes to P.aeruginosa survival under
CC cyanogenic conditions, and thus provides the bacterium with a defense
CC mechanism against endogenous cyanide toxicity (PubMed:17098912). Is the
CC main cytoplasmic rhodanese in P.aeruginosa, accounting for 90% of total
CC rhodanese activity (PubMed:17098912). {ECO:0000269|PubMed:15522204,
CC ECO:0000269|PubMed:17098912}.
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 Evidence={ECO:0000269|PubMed:15522204};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for thiosulfate (at pH 7.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15522204};
CC KM=7.4 mM for thiosulfate (at pH 8.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15522204};
CC KM=12 mM for cyanide (at pH 7.3 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15522204};
CC KM=16 mM for cyanide (at pH 8.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:15522204};
CC Vmax=750 umol/min/mg enzyme (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:15522204};
CC Temperature dependence:
CC Optimum temperature is 20-32 degrees Celsius.
CC {ECO:0000269|PubMed:15522204};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17098912}.
CC -!- INDUCTION: Is constitutively expressed during the entire growth cycle.
CC Expression increases during exponential growth to attain a maximum
CC level at the onset of the stationary phase, slightly decreasing
CC thereafter. {ECO:0000269|PubMed:17098912}.
CC -!- DISRUPTION PHENOTYPE: The growth of a rhdA-deletion mutant is impaired
CC under cyanogenic conditions and fully restored upon complementation
CC with rhdA. When P.aeruginosa cultures are treated with exogenous
CC cyanide, only minor differences in viability between the rhdA-deletion
CC mutant and the wild-type are observed. {ECO:0000269|PubMed:17098912}.
CC -!- BIOTECHNOLOGY: Microbial rhodaneses may contribute to cyanide
CC detoxification in natural environments. {ECO:0000305|PubMed:16307778}.
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DR EMBL; AE004091; AAG08341.1; -; Genomic_DNA.
DR PIR; B83027; B83027.
DR RefSeq; NP_253643.1; NC_002516.2.
DR RefSeq; WP_003113925.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUK9; -.
DR SMR; Q9HUK9; -.
DR STRING; 287.DR97_2309; -.
DR PaxDb; Q9HUK9; -.
DR PRIDE; Q9HUK9; -.
DR DNASU; 879172; -.
DR EnsemblBacteria; AAG08341; AAG08341; PA4956.
DR GeneID; 879172; -.
DR KEGG; pae:PA4956; -.
DR PATRIC; fig|208964.12.peg.5189; -.
DR PseudoCAP; PA4956; -.
DR HOGENOM; CLU_031618_1_7_6; -.
DR InParanoid; Q9HUK9; -.
DR OMA; GYPRVKG; -.
DR PhylomeDB; Q9HUK9; -.
DR BioCyc; PAER208964:G1FZ6-5072-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IMP:PseudoCAP.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Detoxification; Reference proteome; Repeat; Transferase.
FT CHAIN 1..271
FT /note="Thiosulfate sulfurtransferase"
FT /id="PRO_0000439091"
FT DOMAIN 21..129
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 159..270
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 230
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000269|PubMed:15522204"
SQ SEQUENCE 271 AA; 29391 MW; 036F0CF6B3F02251 CRC64;
MSVFSDLPLV IEPSDLAPRL GAPELILVDL TSAARYAEGH IPGARFVDPK RTQWGQPPAP
GLLPAKADLE ALFGELGHRP EATYVVYDDE GGGWAGRFIW LLDVIGHHHY HYLNGGLPAW
IADAQALDRE VPAPVGGPLP LTLHDEPSAT REYLQSRLGA ADLAVWDARN PSEYAGTKVL
AAKAGHVPGA INFEWTAGMD PARALRIRAD IAEVLEDLGI TPDKEVITHC QTHHRSGFTY
LVAKALGYPR VKGYAGSWSE WGNHPDTPVE V
