STR16_ARATH
ID STR16_ARATH Reviewed; 120 AA.
AC Q39129; Q9FKX8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thiosulfate sulfurtransferase 16, chloroplastic;
DE EC=2.8.1.1;
DE AltName: Full=Rhodanese;
DE AltName: Full=Senescence-associated protein;
DE AltName: Full=Sulfurtransferase 16;
DE Short=AtStr16;
GN Name=STR16; OrderedLocusNames=At5g66040; ORFNames=K2A18.11;
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].
RC STRAIN=cv. Landsberg erecta; TISSUE=Seedling;
RA Gachotte D., Benveniste P.;
RT "cDNA obtained by transformation of a yeast sterol mutant erg3 with an
RT Arabidopsis cDNA library and subsequent selection with ketoconazole.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=17088324; DOI=10.1110/ps.062395206;
RA Cornilescu G., Vinarov D.A., Tyler E.M., Markley J.L., Cornilescu C.C.;
RT "Solution structure of a single-domain thiosulfate sulfurtransferase from
RT Arabidopsis thaliana.";
RL Protein Sci. 15:2836-2841(2006).
CC -!- FUNCTION: Thought to act during the early stages of leaf senescence.
CC Catalyzes the transfer of a sulfur ion from a donor to cyanide or to
CC other thiol compounds. Substrate preference is thiosulfate > 3-
CC mercaptopyruvate. {ECO:0000269|PubMed:12482606}.
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:12482606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 mM for thiosulfate {ECO:0000269|PubMed:12482606};
CC KM=51.7 mM for 3-mercaptopyruvate {ECO:0000269|PubMed:12482606};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17088324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15181206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39129-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61433.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X89036; CAA61433.1; ALT_FRAME; mRNA.
DR EMBL; AB011474; BAB10409.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98146.1; -; Genomic_DNA.
DR EMBL; AY049302; AAK83644.1; -; mRNA.
DR EMBL; BT000864; AAN38701.1; -; mRNA.
DR EMBL; AY084763; AAM61332.1; -; mRNA.
DR PIR; S58275; S58275.
DR RefSeq; NP_851278.1; NM_180947.3. [Q39129-1]
DR PDB; 1TQ1; NMR; -; A=2-120.
DR PDBsum; 1TQ1; -.
DR AlphaFoldDB; Q39129; -.
DR BMRB; Q39129; -.
DR SMR; Q39129; -.
DR BioGRID; 21976; 1.
DR STRING; 3702.AT5G66040.1; -.
DR PaxDb; Q39129; -.
DR PRIDE; Q39129; -.
DR ProteomicsDB; 245225; -. [Q39129-1]
DR EnsemblPlants; AT5G66040.1; AT5G66040.1; AT5G66040. [Q39129-1]
DR GeneID; 836734; -.
DR Gramene; AT5G66040.1; AT5G66040.1; AT5G66040. [Q39129-1]
DR KEGG; ath:AT5G66040; -.
DR Araport; AT5G66040; -.
DR TAIR; locus:2156937; AT5G66040.
DR eggNOG; KOG1530; Eukaryota.
DR InParanoid; Q39129; -.
DR OMA; EFSKGHA; -.
DR OrthoDB; 1478958at2759; -.
DR PhylomeDB; Q39129; -.
DR BioCyc; ARA:AT5G66040-MON; -.
DR SABIO-RK; Q39129; -.
DR EvolutionaryTrace; Q39129; -.
DR PRO; PR:Q39129; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39129; baseline and differential.
DR Genevisible; Q39129; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:TAIR.
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; Alternative splicing; Chloroplast; Plastid;
KW Reference proteome; Transferase.
FT CHAIN 1..120
FT /note="Thiosulfate sulfurtransferase 16, chloroplastic"
FT /id="PRO_0000139405"
FT DOMAIN 20..120
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 80
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 3
FT /note="E -> D (in Ref. 1; CAA61433)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1TQ1"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1TQ1"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1TQ1"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:1TQ1"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1TQ1"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1TQ1"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1TQ1"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1TQ1"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1TQ1"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:1TQ1"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:1TQ1"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1TQ1"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1TQ1"
SQ SEQUENCE 120 AA; 12676 MW; 81CAE9D3C2DFCAFE CRC64;
MAEESRVPSS VSVTVAHDLL LAGHRYLDVR TPEEFSQGHA CGAINVPYMN RGASGMSKNP
DFLEQVSSHF GQSDNIIVGC QSGGRSIKAT TDLLHAGFTG VKDIVGGYSA WAKNGLPTKA
