STR2_ARATH
ID STR2_ARATH Reviewed; 342 AA.
AC Q24JL3; Q0WQ03; Q9M4F7; Q9S7Y9; Q9SA45;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Thiosulfate/3-mercaptopyruvate sulfurtransferase 2;
DE EC=2.8.1.1 {ECO:0000269|PubMed:10951223};
DE EC=2.8.1.2 {ECO:0000269|PubMed:10951223};
DE AltName: Full=Rhodanese homolog protein 2;
DE Short=AtRDH2;
DE AltName: Full=Sulfurtransferase 2;
DE Short=AtStr2;
GN Name=STR2; Synonyms=RDH2; OrderedLocusNames=At1g16460; ORFNames=F3O9.26;
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 2), 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).
RX PubMed=10951216; DOI=10.1046/j.1432-1327.2000.01623.x;
RA Papenbrock J., Schmidt A.;
RT "Characterization of two sulfurtransferase isozymes from Arabidopsis
RT thaliana.";
RL Eur. J. Biochem. 267:5571-5579(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), 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 [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [9]
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 [10]
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 [11]
RP FUNCTION, 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).
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:10951223,
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;
CC Evidence={ECO:0000269|PubMed:10951223};
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:10951223};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 mM for thiosulfate {ECO:0000269|PubMed:10951223};
CC KM=72 mM for sodium mercaptopyruvate {ECO:0000269|PubMed:10951223};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10734224,
CC ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:15181206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q24JL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q24JL3-2; Sequence=VSP_042634;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:10951223}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:21189252}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34697.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB88023.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010500; CAB53639.1; -; mRNA.
DR EMBL; AJ243888; CAB88023.1; ALT_FRAME; mRNA.
DR EMBL; AB032865; BAA85149.1; -; mRNA.
DR EMBL; AC006341; AAD34697.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29453.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29454.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29455.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29456.1; -; Genomic_DNA.
DR EMBL; BT024876; ABD85147.1; -; mRNA.
DR EMBL; AK228907; BAF00796.1; -; mRNA.
DR EMBL; AK229282; BAF01145.1; -; mRNA.
DR EMBL; AY084558; AAM61125.1; -; mRNA.
DR PIR; A86300; A86300.
DR PIR; T52655; T52655.
DR PIR; T52663; T52663.
DR RefSeq; NP_001031056.1; NM_001035979.1. [Q24JL3-2]
DR RefSeq; NP_001185012.1; NM_001198083.1. [Q24JL3-2]
DR RefSeq; NP_563998.1; NM_101511.6. [Q24JL3-2]
DR RefSeq; NP_849675.1; NM_179344.2. [Q24JL3-1]
DR AlphaFoldDB; Q24JL3; -.
DR SMR; Q24JL3; -.
DR STRING; 3702.AT1G16460.2; -.
DR PaxDb; Q24JL3; -.
DR PRIDE; Q24JL3; -.
DR ProteomicsDB; 228365; -. [Q24JL3-1]
DR EnsemblPlants; AT1G16460.1; AT1G16460.1; AT1G16460. [Q24JL3-2]
DR EnsemblPlants; AT1G16460.2; AT1G16460.2; AT1G16460. [Q24JL3-1]
DR EnsemblPlants; AT1G16460.3; AT1G16460.3; AT1G16460. [Q24JL3-2]
DR EnsemblPlants; AT1G16460.4; AT1G16460.4; AT1G16460. [Q24JL3-2]
DR GeneID; 838216; -.
DR Gramene; AT1G16460.1; AT1G16460.1; AT1G16460. [Q24JL3-2]
DR Gramene; AT1G16460.2; AT1G16460.2; AT1G16460. [Q24JL3-1]
DR Gramene; AT1G16460.3; AT1G16460.3; AT1G16460. [Q24JL3-2]
DR Gramene; AT1G16460.4; AT1G16460.4; AT1G16460. [Q24JL3-2]
DR KEGG; ath:AT1G16460; -.
DR Araport; AT1G16460; -.
DR TAIR; locus:2032800; AT1G16460.
DR eggNOG; KOG1529; Eukaryota.
DR InParanoid; Q24JL3; -.
DR OMA; HIPRSKC; -.
DR OrthoDB; 1553525at2759; -.
DR PhylomeDB; Q24JL3; -.
DR BioCyc; ARA:AT1G16460-MON; -.
DR BRENDA; 2.8.1.1; 399.
DR BRENDA; 2.8.1.2; 399.
DR SABIO-RK; Q24JL3; -.
DR PRO; PR:Q24JL3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q24JL3; baseline and differential.
DR Genevisible; Q24JL3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016784; F:3-mercaptopyruvate 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; IGI: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; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Reference proteome; Repeat; Transferase.
FT CHAIN 1..342
FT /note="Thiosulfate/3-mercaptopyruvate sulfurtransferase 2"
FT /id="PRO_0000416526"
FT DOMAIN 56..173
FT /note="Rhodanese 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 224..338
FT /note="Rhodanese 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 298
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10734224,
FT ECO:0000303|PubMed:10951223, ECO:0000303|Ref.7"
FT /id="VSP_042634"
FT CONFLICT 94
FT /note="N -> D (in Ref. 2; CAB88023)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..105
FT /note="NLRH -> KLHP (in Ref. 2; CAB88023)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="E -> G (in Ref. 7; BAF00796)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="T -> I (in Ref. 7; BAF00796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 37412 MW; CE8034647B9A766A CRC64;
MKRAFSSQLR SAYPASKSTH FGRVMASSGS EAKANYAPIS TNEPVVSVDW LHSNLGDADI
KVLDASWYMA HEQRNPIQEY QVAHIPGALF FDLNGIADRK TNLRHMLPSE EAFAAGCSAL
GIENNDGVVV YDGMGLFSAA RVWWMFRVFG HDKVWVLDGG LPKWRASGYD VESSVSNDAI
LKASAATEAI EKIYQGQTIS PITFQTKFRP HLVLALDQVK ENIEDKTYQH IDARSKARFD
GIAPEPWKGL PSGHIPGSKC VPFPLMFDSS QTLLPAEELK KQFEQEDISL DSPIAASCGT
GVTACILALG LYRLGKTNVA IYDGSWTEWA TAPNLPIVGS SS
