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 01-MAY-2013, entry version 91.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
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
RT physically assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT various 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.,
RA Cornilescu C.C.;
RT "Solution structure of a single-domain thiosulfate sulfurtransferase
RT from Arabidopsis thaliana.";
RL Protein Sci. 15:2836-2841(2006).
CC -!- FUNCTION: Thought to act during the early stages of leaf
CC senescence. Catalyzes the transfer of a sulfur ion from a donor to
CC cyanide or to other thiol compounds. Substrate preference is
CC thiosulfate > 3-mercaptopyruvate.
CC -!- CATALYTIC ACTIVITY: Thiosulfate + cyanide = sulfite + thiocyanate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 mM for thiosulfate;
CC KM=51.7 mM for 3-mercaptopyruvate;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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 -!- SIMILARITY: Contains 1 rhodanese domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA61433.1; Type=Frameshift; Positions=40, 43, 116;
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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 IPI; IPI00531957; -.
DR PIR; S58275; S58275.
DR RefSeq; NP_851278.1; NM_180947.2.
DR UniGene; At.23333; -.
DR PDB; 1TQ1; NMR; -; A=2-120.
DR PDBsum; 1TQ1; -.
DR ProteinModelPortal; Q39129; -.
DR SMR; Q39129; 2-119.
DR PaxDb; Q39129; -.
DR PRIDE; Q39129; -.
DR EnsemblPlants; AT5G66040.1; AT5G66040.1; AT5G66040.
DR GeneID; 836734; -.
DR KEGG; ath:AT5G66040; -.
DR GeneFarm; 4731; -.
DR TAIR; At5g66040; -.
DR eggNOG; COG0607; -.
DR HOGENOM; HOG000247776; -.
DR InParanoid; Q39129; -.
DR OMA; CGAINVP; -.
DR PhylomeDB; Q39129; -.
DR BRENDA; 2.8.1.1; 399.
DR SABIO-RK; Q39129; -.
DR EvolutionaryTrace; Q39129; -.
DR ArrayExpress; Q39129; -.
DR Genevestigator; Q39129; -.
DR GO; GO:0009507; C:chloroplast; IDA: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 Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese-like; 1.
DR PROSITE; PS00380; RHODANESE_1; FALSE_NEG.
DR PROSITE; PS00683; RHODANESE_2; FALSE_NEG.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Complete proteome;
KW Plastid; Reference proteome; Transferase.
FT CHAIN 1 120 Thiosulfate sulfurtransferase 16,
FT chloroplastic.
FT /FTId=PRO_0000139405.
FT DOMAIN 20 120 Rhodanese.
FT ACT_SITE 80 80 Cysteine persulfide intermediate (By
FT similarity).
FT BINDING 85 85 Substrate (By similarity).
FT CONFLICT 3 3 E -> D (in Ref. 1; CAA61433).
FT STRAND 9 12
FT HELIX 13 22
FT STRAND 26 30
FT HELIX 32 37
FT STRAND 43 45
FT TURN 53 55
FT TURN 59 61
FT HELIX 62 66
FT TURN 67 69
FT STRAND 74 82
FT HELIX 85 97
FT STRAND 100 105
FT HELIX 108 114
SQ SEQUENCE 120 AA; 12676 MW; 81CAE9D3C2DFCAFE CRC64;
MAEESRVPSS VSVTVAHDLL LAGHRYLDVR TPEEFSQGHA CGAINVPYMN RGASGMSKNP
DFLEQVSSHF GQSDNIIVGC QSGGRSIKAT TDLLHAGFTG VKDIVGGYSA WAKNGLPTKA
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