THTR_YEAST
ID THTR_YEAST Reviewed; 304 AA.
AC Q08686; D6W2V2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Thiosulfate sulfurtransferase TUM1;
DE EC=2.8.1.1;
DE AltName: Full=Thiouridine modification protein 1;
GN Name=TUM1; OrderedLocusNames=YOR251C;
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=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
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 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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP FUNCTION.
RX PubMed=18755837; DOI=10.1261/rna.1184108;
RA Huang B., Lu J., Bystroem A.S.;
RT "A genome-wide screen identifies genes required for formation of the wobble
RT nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces
RT cerevisiae.";
RL RNA 14:2183-2194(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, 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).
CC -!- FUNCTION: Required for formation of the 2-thio group of the 5-
CC methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.
CC {ECO:0000269|PubMed:18755837}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure conformations
CC suggesting a common evolutionary origin. Only the C-terminal rhodanese
CC domain contains the catalytic cysteine residue (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 5770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z75159; CAA99473.1; -; Genomic_DNA.
DR EMBL; AY692732; AAT92751.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11018.1; -; Genomic_DNA.
DR PIR; S67148; S67148.
DR RefSeq; NP_014894.3; NM_001183670.3.
DR PDB; 3UTN; X-ray; 1.90 A; X=1-304.
DR PDBsum; 3UTN; -.
DR AlphaFoldDB; Q08686; -.
DR SMR; Q08686; -.
DR BioGRID; 34641; 111.
DR DIP; DIP-4457N; -.
DR IntAct; Q08686; 9.
DR STRING; 4932.YOR251C; -.
DR iPTMnet; Q08686; -.
DR MaxQB; Q08686; -.
DR PaxDb; Q08686; -.
DR PRIDE; Q08686; -.
DR EnsemblFungi; YOR251C_mRNA; YOR251C; YOR251C.
DR GeneID; 854425; -.
DR KEGG; sce:YOR251C; -.
DR SGD; S000005777; TUM1.
DR VEuPathDB; FungiDB:YOR251C; -.
DR eggNOG; KOG1529; Eukaryota.
DR GeneTree; ENSGT00510000046773; -.
DR HOGENOM; CLU_031618_3_0_1; -.
DR InParanoid; Q08686; -.
DR OMA; QRPGHVP; -.
DR BioCyc; MetaCyc:YOR251C-MON; -.
DR BioCyc; YEAST:YOR251C-MON; -.
DR Reactome; R-SCE-1614558; Degradation of cysteine and homocysteine.
DR PRO; PR:Q08686; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08686; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:SGD.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IMP:SGD.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:SGD.
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 InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364; PTHR11364; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Mitochondrion; Phosphoprotein; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..304
FT /note="Thiosulfate sulfurtransferase TUM1"
FT /id="PRO_0000139402"
FT DOMAIN 20..137
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 177..299
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 191..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 259
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:3UTN"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:3UTN"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:3UTN"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:3UTN"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3UTN"
SQ SEQUENCE 304 AA; 34219 MW; F8082DF7CC279E82 CRC64;
MPLFDLISPK AFVKLVASEK VHRIVPVDAT WYLPSWKLDN KVDFLTKPRI PNSIFFDIDA
ISDKKSPYPH MFPTKKVFDD AMSNLGVQKD DILVVYDRVG NFSSPRCAWT LGVMGHPKVY
LLNNFNQYRE FKYPLDSSKV AAFSPYPKSH YESSESFQDK EIVDYEEMFQ LVKSGELAKK
FNAFDARSLG RFEGTEPEPR SDIPSGHIPG TQPLPYGSLL DPETKTYPEA GEAIHATLEK
ALKDFHCTLD PSKPTICSCG TGVSGVIIKT ALELAGVPNV RLYDGSWTEW VLKSGPEWIA
ENRD
