STR18_ARATH
ID STR18_ARATH Reviewed; 136 AA.
AC Q9FKW8; Q8LCX9;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Thiosulfate sulfurtransferase 18;
DE EC=2.8.1.1;
DE AltName: Full=Sulfurtransferase 18;
DE Short=AtStr18;
GN Name=STR18; OrderedLocusNames=At5g66170; ORFNames=K2A18.25;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: 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. {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=1.1 mM for thiosulfate {ECO:0000269|PubMed:12482606};
CC KM=35.4 mM for 3-mercaptopyruvate {ECO:0000269|PubMed:12482606};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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=Q9FKW8-1; Sequence=Displayed;
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DR EMBL; AB011474; BAB10422.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98170.1; -; Genomic_DNA.
DR EMBL; AY065058; AAL57692.1; -; mRNA.
DR EMBL; AY091669; AAM10268.1; -; mRNA.
DR EMBL; AK222135; BAD95161.1; -; mRNA.
DR EMBL; AY086338; AAM64406.1; -; mRNA.
DR RefSeq; NP_001190631.1; NM_001203702.1. [Q9FKW8-1]
DR AlphaFoldDB; Q9FKW8; -.
DR SMR; Q9FKW8; -.
DR STRING; 3702.AT5G66170.2; -.
DR PaxDb; Q9FKW8; -.
DR PRIDE; Q9FKW8; -.
DR ProteomicsDB; 228273; -. [Q9FKW8-1]
DR EnsemblPlants; AT5G66170.3; AT5G66170.3; AT5G66170. [Q9FKW8-1]
DR GeneID; 836749; -.
DR Gramene; AT5G66170.3; AT5G66170.3; AT5G66170. [Q9FKW8-1]
DR KEGG; ath:AT5G66170; -.
DR Araport; AT5G66170; -.
DR eggNOG; KOG1530; Eukaryota.
DR InParanoid; Q9FKW8; -.
DR OMA; SACDKEE; -.
DR BRENDA; 2.8.1.1; 399.
DR SABIO-RK; Q9FKW8; -.
DR PRO; PR:Q9FKW8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKW8; baseline and differential.
DR Genevisible; Q9FKW8; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:UniProtKB.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR044684; STR17/STR18/HARC1-like.
DR PANTHER; PTHR44542; PTHR44542; 1.
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 Alternative splicing; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..136
FT /note="Thiosulfate sulfurtransferase 18"
FT /id="PRO_0000416538"
FT DOMAIN 26..128
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 88
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT CONFLICT 68
FT /note="Q -> R (in Ref. 5; AAM64406)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="T -> K (in Ref. 5; AAM64406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 14883 MW; 6530E5E7D1B7BC64 CRC64;
MSQSISSSTK AEEVVSVDVS QAKTLLQSGH QYLDVRTQDE FRRGHCEAAK IVNIPYMLNT
PQGRVKNQEF LEQVSSLLNP ADDILVGCQS GARSLKATTE LVAAGYKKVR NVGGGYLAWV
DHSFPINTEE EEPSAN
