RDL1_YEAST
ID RDL1_YEAST Reviewed; 139 AA.
AC Q12305; D6W2Y3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Thiosulfate:glutathione sulfurtransferase {ECO:0000303|PubMed:24981631};
DE Short=TST {ECO:0000303|PubMed:24981631};
DE EC=2.8.1.- {ECO:0000269|PubMed:24981631};
DE AltName: Full=Rhodanese-like protein 1;
GN Name=RDL1; OrderedLocusNames=YOR285W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [8]
RP IDENTIFICATION.
RX PubMed=19864628; DOI=10.1073/pnas.0900729106;
RA Foster M.W., Forrester M.T., Stamler J.S.;
RT "A protein microarray-based analysis of S-nitrosylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18948-18953(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP CYS-98, ACTIVITY REGULATION, AND ACTIVE SITE.
RX PubMed=24981631; DOI=10.1021/bi500650h;
RA Melideo S.L., Jackson M.R., Jorns M.S.;
RT "Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a
RT novel human sulfurtransferase and its yeast ortholog.";
RL Biochemistry 53:4739-4753(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "Atomic resolution structure of uncharacterized protein from saccharomyces
RT cerevisiae.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Thiosulfate:glutathione sulfurtransferase (TST) required to
CC produce S-sulfanylglutathione (GSS(-)), a central intermediate in
CC hydrogen sulfide metabolism (PubMed:24981631). Provides the link
CC between the first step in H(2)S metabolism performed by the
CC sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of
CC H(2)S to thiosulfate, and the sulfur dioxygenase (SDO) which uses
CC GSS(-) as substrate (PubMed:24981631). The thermodynamic coupling of
CC the irreversible SDO and reversible TST reactions provides a model for
CC the physiologically relevant reaction with thiosulfate as the sulfane
CC donor (PubMed:24981631). {ECO:0000269|PubMed:24981631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + thiosulfate = H(+) + S-sulfanylglutathione +
CC sulfite; Xref=Rhea:RHEA:55976, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:33542, ChEBI:CHEBI:57925, ChEBI:CHEBI:58905;
CC Evidence={ECO:0000269|PubMed:24981631};
CC -!- ACTIVITY REGULATION: GSS(-) is a potent inhibitor of RDL1, since the
CC presence of the sulfur dioxygenase strongly increases the RDL1
CC catalytic activity (PubMed:24981631). {ECO:0000269|PubMed:24981631}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.6 mM for glutathione {ECO:0000269|PubMed:24981631};
CC KM=2.0 mM for thiosulfate {ECO:0000269|PubMed:24981631};
CC KM=0.2 mM for glutathione (in the presence of sulfur dioxygenase)
CC {ECO:0000269|PubMed:24981631};
CC KM=7.6 mM for thiosulfate (in the presence of sulfur dioxygenase)
CC {ECO:0000269|PubMed:24981631};
CC KM=3.1 mM for thiosulfate (when glutathione is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=5.5 mM for thiosulfate (when cystein is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=4.3 mM for thiosulfate (when coenzyme A is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=3.1 mM for thiosulfate (when DTT is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=4.0 mM for thiosulfate (when cyanide is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=5.6 mM for glutathione (when thiosulfate is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=2.9 mM for cystein (when thiosulfate is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=0.15 mM for coenzyme A (when thiosulfate is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=0.16 mM for DTT (when thiosulfate is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC KM=2.6 mM for cyanide (when thiosulfate is the acceptor)
CC {ECO:0000269|PubMed:24981631};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}.
CC -!- MISCELLANEOUS: Present with 7470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X89633; CAA61789.1; -; Genomic_DNA.
DR EMBL; Z75193; CAA99512.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11049.1; -; Genomic_DNA.
DR PIR; S67187; S67187.
DR RefSeq; NP_014928.1; NM_001183704.1.
DR PDB; 3D1P; X-ray; 0.98 A; A=1-139.
DR PDBsum; 3D1P; -.
DR AlphaFoldDB; Q12305; -.
DR SMR; Q12305; -.
DR BioGRID; 34672; 115.
DR DIP; DIP-4086N; -.
DR IntAct; Q12305; 1.
DR STRING; 4932.YOR285W; -.
DR iPTMnet; Q12305; -.
DR MaxQB; Q12305; -.
DR PaxDb; Q12305; -.
DR PRIDE; Q12305; -.
DR TopDownProteomics; Q12305; -.
DR DNASU; 854459; -.
DR EnsemblFungi; YOR285W_mRNA; YOR285W; YOR285W.
DR GeneID; 854459; -.
DR KEGG; sce:YOR285W; -.
DR SGD; S000005811; RDL1.
DR VEuPathDB; FungiDB:YOR285W; -.
DR eggNOG; KOG1530; Eukaryota.
DR GeneTree; ENSGT00940000163155; -.
DR HOGENOM; CLU_089574_0_2_1; -.
DR InParanoid; Q12305; -.
DR OMA; FFCQMGR; -.
DR BioCyc; MetaCyc:G3O-33771-MON; -.
DR BioCyc; YEAST:G3O-33771-MON; -.
DR EvolutionaryTrace; Q12305; -.
DR PRO; PR:Q12305; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12305; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:SGD.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..139
FT /note="Thiosulfate:glutathione sulfurtransferase"
FT /id="PRO_0000245269"
FT DOMAIN 37..138
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 98
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173,
FT ECO:0000269|PubMed:24981631"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 98
FT /note="C->A,S: Leads to the loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24981631"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:3D1P"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3D1P"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:3D1P"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3D1P"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3D1P"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3D1P"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3D1P"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3D1P"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:3D1P"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3D1P"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3D1P"
FT HELIX 125..131
FT /evidence="ECO:0007829|PDB:3D1P"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3D1P"
SQ SEQUENCE 139 AA; 15413 MW; 715DD12210E3B35E CRC64;
MWKAVMNAWN GTESQSKNVS NIQSYSFEDM KRIVGKHDPN VVLVDVREPS EYSIVHIPAS
INVPYRSHPD AFALDPLEFE KQIGIPKPDS AKELIFYCAS GKRGGEAQKV ASSHGYSNTS
LYPGSMNDWV SHGGDKLDL
