STR1_ARATH
ID STR1_ARATH Reviewed; 379 AA.
AC O64530; A8MSC9; Q9SCY8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thiosulfate/3-mercaptopyruvate sulfurtransferase 1, mitochondrial;
DE EC=2.8.1.1 {ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
DE EC=2.8.1.2 {ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
DE AltName: Full=AtMST1;
DE AltName: Full=Rhodanese homolog protein 1;
DE Short=AtRDH1;
DE AltName: Full=Sulfurtransferase 1;
DE Short=AtStr1;
DE Flags: Precursor;
GN Name=STR1; Synonyms=MST1, RDH1, ST1; OrderedLocusNames=At1g79230;
GN ORFNames=YUP8H12R.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10734224; DOI=10.1016/s0014-5793(00)01311-9;
RA Hatzfeld Y., Saito K.;
RT "Evidence for the existence of rhodanese (thiosulfate:cyanide
RT sulfurtransferase) in plants: preliminary characterization of two rhodanese
RT cDNAs from Arabidopsis thaliana.";
RL FEBS Lett. 470:147-150(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10601861; DOI=10.1046/j.1432-1327.2000.00980.x;
RA Papenbrock J., Schmidt A.;
RT "Characterization of a sulfurtransferase from Arabidopsis thaliana.";
RL Eur. J. Biochem. 267:145-154(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10951223; DOI=10.1046/j.1432-1327.2000.01633.x;
RA Nakamura T., Yamaguchi Y., Sano H.;
RT "Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular
RT localization and enzymatic activities.";
RL Eur. J. Biochem. 267:5621-5630(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-152; CYS-295; CYS-305; CYS-333 AND CYS-340.
RX PubMed=12437129; DOI=10.1515/bc.2002.155;
RA Burow M., Kessler D., Papenbrock J.;
RT "Enzymatic activity of the Arabidopsis sulfurtransferase resides in the C-
RT terminal domain but is boosted by the N-terminal domain and the linker
RT peptide in the full-length enzyme.";
RL Biol. Chem. 383:1363-1372(2002).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12482606; DOI=10.1016/s0014-5793(02)03723-7;
RA Bauer M., Papenbrock J.;
RT "Identification and characterization of single-domain thiosulfate
RT sulfurtransferases from Arabidopsis thaliana.";
RL FEBS Lett. 532:427-431(2002).
RN [12]
RP INDUCTION.
RX PubMed=12721843; DOI=10.1007/s00425-002-0964-5;
RA Meyer T., Burow M., Bauer M., Papenbrock J.;
RT "Arabidopsis sulfurtransferases: investigation of their function during
RT senescence and in cyanide detoxification.";
RL Planta 217:1-10(2003).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15181206; DOI=10.1104/pp.104.040121;
RA Bauer M., Dietrich C., Nowak K., Sierralta W.D., Papenbrock J.;
RT "Intracellular localization of Arabidopsis sulfurtransferases.";
RL Plant Physiol. 135:916-926(2004).
RN [14]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
RA Bartels A., Mock H.P., Papenbrock J.;
RT "Differential expression of Arabidopsis sulfurtransferases under various
RT growth conditions.";
RL Plant Physiol. Biochem. 45:178-187(2007).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21189252; DOI=10.1074/jbc.m110.182865;
RA Mao G., Wang R., Guan Y., Liu Y., Zhang S.;
RT "Sulfurtransferases 1 and 2 play essential roles in embryo and seed
RT development in Arabidopsis thaliana.";
RL J. Biol. Chem. 286:7548-7557(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-57, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ARG-56, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the transfer of a sulfur ion from a donor to
CC cyanide or to other thiol compounds. Substrate preference is 3-
CC mercaptopyruvate > thiosulfate. Involved in embryo and seed
CC development. {ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606,
CC ECO:0000269|PubMed:21189252}.
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; Evidence={ECO:0000269|PubMed:10601861,
CC ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129,
CC ECO:0000269|PubMed:12482606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol =
CC [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate;
CC Xref=Rhea:RHEA:21740, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57678; EC=2.8.1.2;
CC Evidence={ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for thiosulfate {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC KM=0.7 mM for thiosulfate {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC KM=1.7 mM for thiosulfate {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC KM=3.4 mM for 3-mercaptopyruvate {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC KM=3.7 mM for 3-mercaptopyruvate {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC KM=11 mM for sodium mercaptopyruvate {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10601861,
CC ECO:0000269|PubMed:10734224, ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:15181206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64530-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64530-2; Sequence=VSP_042633;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:10951223,
CC ECO:0000269|PubMed:21189252}.
CC -!- INDUCTION: Induced during senescence. {ECO:0000269|PubMed:12721843}.
CC -!- DISRUPTION PHENOTYPE: Shrunken seeds with unmature embryos.
CC {ECO:0000269|PubMed:21189252}.
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DR EMBL; AJ011045; CAB55306.1; -; mRNA.
DR EMBL; AJ131404; CAB64716.1; -; mRNA.
DR EMBL; AB032864; BAA85148.1; -; mRNA.
DR EMBL; AC002986; AAC17062.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36219.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36221.1; -; Genomic_DNA.
DR EMBL; AK118208; BAC42830.1; -; mRNA.
DR EMBL; AY075685; AAL77692.1; -; mRNA.
DR EMBL; BT026029; ABG48385.1; -; mRNA.
DR EMBL; AY087137; AAM64695.1; -; mRNA.
DR PIR; T01034; T01034.
DR PIR; T52658; T52658.
DR RefSeq; NP_001077848.1; NM_001084379.1. [O64530-2]
DR RefSeq; NP_565203.1; NM_106574.3. [O64530-1]
DR AlphaFoldDB; O64530; -.
DR SMR; O64530; -.
DR STRING; 3702.AT1G79230.1; -.
DR iPTMnet; O64530; -.
DR MetOSite; O64530; -.
DR SwissPalm; O64530; -.
DR PaxDb; O64530; -.
DR PRIDE; O64530; -.
DR ProteomicsDB; 228364; -. [O64530-1]
DR EnsemblPlants; AT1G79230.1; AT1G79230.1; AT1G79230. [O64530-1]
DR EnsemblPlants; AT1G79230.3; AT1G79230.3; AT1G79230. [O64530-2]
DR GeneID; 844264; -.
DR Gramene; AT1G79230.1; AT1G79230.1; AT1G79230. [O64530-1]
DR Gramene; AT1G79230.3; AT1G79230.3; AT1G79230. [O64530-2]
DR KEGG; ath:AT1G79230; -.
DR Araport; AT1G79230; -.
DR TAIR; locus:2207345; AT1G79230.
DR eggNOG; KOG1529; Eukaryota.
DR InParanoid; O64530; -.
DR OrthoDB; 1553525at2759; -.
DR PhylomeDB; O64530; -.
DR BioCyc; ARA:AT1G79230-MON; -.
DR SABIO-RK; O64530; -.
DR PRO; PR:O64530; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64530; baseline and differential.
DR Genevisible; O64530; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IDA:TAIR.
DR GO; GO:0016783; F:sulfurtransferase activity; IDA:TAIR.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
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 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 Acetylation; Alternative splicing; Mitochondrion; Pyruvate;
KW Reference proteome; Repeat; Transferase; Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 57..379
FT /note="Thiosulfate/3-mercaptopyruvate sulfurtransferase 1,
FT mitochondrial"
FT /id="PRO_0000416525"
FT DOMAIN 91..208
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 259..373
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 333
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT MOD_RES 57
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042633"
FT MUTAGEN 152
FT /note="C->A: Slight reduction of sulfurtransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:12437129"
FT MUTAGEN 295
FT /note="C->N: Slight reduction of sulfurtransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:12437129"
FT MUTAGEN 305
FT /note="C->E: Slight reduction of sulfurtransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:12437129"
FT MUTAGEN 333
FT /note="C->S: Loss of sulfurtransferase and 3-
FT mercaptopyruvate sulfurtransferase activities."
FT /evidence="ECO:0000269|PubMed:12437129"
FT MUTAGEN 340
FT /note="C->V: Reduces thiosulfate sulfurtransferase activity
FT 4-fold. Slight reduction of 3-mercaptopyruvate
FT sulfurtransferase activity."
FT /evidence="ECO:0000269|PubMed:12437129"
FT CONFLICT 114
FT /note="E -> D (in Ref. 2; CAB64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..139
FT /note="SLP -> TFA (in Ref. 2; CAB64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="Missing (in Ref. 2; CAB64716)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> S (in Ref. 2; CAB64716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 41893 MW; 2268F7A5F2DA62B6 CRC64;
MASTLFSRTF LAASHRLITP SLPQKIFNPA TFLSRSLHSQ LGSASTAYKS TTWARRAMAS
TGVETKAGYS TSSVSTSEPV VSVDWLHANL REPDLKILDA SWYMPDEQRN PIQEYQVAHI
PRALFFDLDG ISDRKTSLPH MLPTEEAFAA GCSALGIDNK DEVVVYDGKG IFSAARVWWM
FRVFGHEKVW VLDGGLPRWR ASGYDVESSA SGDAILKASA ASEAIEKIYQ GQTVSPITFQ
TKFQPHLVWT LDQVKNNMED PTYQHIDARS KARFDGTAPE PRKGIRSGHI PGSKCIPFPQ
MFDSCNTLLP AEELKKRFDQ EDISLDKPIM ASCGTGVTAC ILAMGLHRLG KTDVPIYDGS
WTEWATQPDL PIESVESSS
