RDL2_YEAST
ID RDL2_YEAST Reviewed; 149 AA.
AC Q08742; D6W2Y4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Thiosulfate sulfurtransferase RDL2, mitochondrial;
DE EC=2.8.1.1 {ECO:0000269|PubMed:19864628};
DE AltName: Full=Altered inheritance of mitochondria protein 42;
DE AltName: Full=Found in mitochondrial proteome protein 31;
DE AltName: Full=Rhodanese-like protein 2;
DE Flags: Precursor;
GN Name=RDL2; Synonyms=AIM42, FMP31; OrderedLocusNames=YOR286W;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Thiosulfate sulfurtransferase which catalyzes the transfer of
CC sulfane sulfur from thiosulfate to cyanide.
CC {ECO:0000269|PubMed:19864628}.
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:19864628};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16882;
CC Evidence={ECO:0000305|PubMed:19864628};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC {ECO:0000269|PubMed:19300474}.
CC -!- MISCELLANEOUS: Present with 4220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z75194; CAA99513.1; -; Genomic_DNA.
DR EMBL; AY692684; AAT92703.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11050.1; -; Genomic_DNA.
DR PIR; S67188; S67188.
DR RefSeq; NP_014929.3; NM_001183705.3.
DR PDB; 6K6R; X-ray; 2.47 A; A/D=1-149.
DR PDBsum; 6K6R; -.
DR AlphaFoldDB; Q08742; -.
DR SMR; Q08742; -.
DR BioGRID; 34673; 66.
DR DIP; DIP-4456N; -.
DR IntAct; Q08742; 1.
DR STRING; 4932.YOR286W; -.
DR MaxQB; Q08742; -.
DR PaxDb; Q08742; -.
DR PRIDE; Q08742; -.
DR EnsemblFungi; YOR286W_mRNA; YOR286W; YOR286W.
DR GeneID; 854460; -.
DR KEGG; sce:YOR286W; -.
DR SGD; S000005812; RDL2.
DR VEuPathDB; FungiDB:YOR286W; -.
DR eggNOG; KOG1530; Eukaryota.
DR GeneTree; ENSGT00940000163155; -.
DR HOGENOM; CLU_089574_0_2_1; -.
DR InParanoid; Q08742; -.
DR OMA; CHNFCTA; -.
DR BioCyc; MetaCyc:G3O-33772-MON; -.
DR BioCyc; YEAST:G3O-33772-MON; -.
DR PRO; PR:Q08742; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08742; protein.
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; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..149
FT /note="Thiosulfate sulfurtransferase RDL2, mitochondrial"
FT /id="PRO_0000245268"
FT DOMAIN 45..146
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 106
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:6K6R"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6K6R"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6K6R"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6K6R"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6K6R"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:6K6R"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:6K6R"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6K6R"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:6K6R"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6K6R"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:6K6R"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6K6R"
SQ SEQUENCE 149 AA; 16697 MW; 8BF91B05233CB81F CRC64;
MFKHSTGILS RTVSARSPTL VLRTFTTKAP KIYTFDQVRN LVEHPNDKKL LVDVREPKEV
KDYKMPTTIN IPVNSAPGAL GLPEKEFHKV FQFAKPPHDK ELIFLCAKGV RAKTAEELAR
SYGYENTGIY PGSITEWLAK GGADVKPKK
