HOL1_ARATH
ID HOL1_ARATH Reviewed; 227 AA.
AC Q0WP12; C0Z3K5; O80561;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Thiocyanate methyltransferase 1 {ECO:0000303|PubMed:19419967};
DE EC=2.1.1.n4 {ECO:0000255|PROSITE-ProRule:PRU00918, ECO:0000269|PubMed:19419967};
DE AltName: Full=Protein HARMLESS TO OZONE LAYER 1 {ECO:0000303|PubMed:14561407};
DE Short=AtHOL1 {ECO:0000303|PubMed:14561407};
GN Name=HOL1 {ECO:0000303|PubMed:14561407};
GN OrderedLocusNames=At2g43910 {ECO:0000312|Araport:AT2G43910};
GN ORFNames=F6E13.4 {ECO:0000312|EMBL:AAC23400.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14561407; DOI=10.1016/j.cub.2003.09.055;
RA Rhew R.C., Ostergaard L., Saltzman E.S., Yanofsky M.F.;
RT "Genetic control of methyl halide production in Arabidopsis.";
RL Curr. Biol. 13:1809-1813(2003).
RN [8]
RP FUNCTION.
RA Nagatoshi Y., Nakamura T.;
RT "Characterization of three halide methyltransferases in Arabidopsis
RT thaliana.";
RL Plant Biotechnol. 24:503-506(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19419967; DOI=10.1074/jbc.m109.001032;
RA Nagatoshi Y., Nakamura T.;
RT "Arabidopsis HARMLESS TO OZONE LAYER protein methylates a glucosinolate
RT breakdown product and functions in resistance to Pseudomonas syringae pv.
RT maculicola.";
RL J. Biol. Chem. 284:19301-19309(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-227 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RX PubMed=20376845; DOI=10.1002/anie.201000119;
RA Schmidberger J.W., James A.B., Edwards R., Naismith J.H., O'Hagan D.;
RT "Halomethane biosynthesis: structure of a SAM-dependent halide
RT methyltransferase from Arabidopsis thaliana.";
RL Angew. Chem. Int. Ed. Engl. 49:3646-3648(2010).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase. Involved
CC in glucosinolate metabolism and defense against phytopathogens. Highly
CC reactive to thiocyanate (NCS(-)) derived from myrosinase-mediated
CC hydrolysis of glucosinolates upon tissue damage.
CC {ECO:0000269|PubMed:19419967, ECO:0000269|Ref.8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + thiocyanate = methyl thiocyanate +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:28014, ChEBI:CHEBI:18022,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61112; EC=2.1.1.n4;
CC Evidence={ECO:0000269|PubMed:19419967};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 uM for KSCN {ECO:0000269|PubMed:19419967};
CC KM=280 mM for KCL {ECO:0000269|PubMed:19419967};
CC KM=0.26 mM for ammonium sulfide {ECO:0000269|PubMed:19419967};
CC KM=92 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19419967};
CC Vmax=2.2 umol/sec/mg enzyme toward KSCN
CC {ECO:0000269|PubMed:19419967};
CC Vmax=82 nmol/sec/mg enzyme toward KCL {ECO:0000269|PubMed:19419967};
CC Vmax=2.6 umol/sec/mg enzyme toward ammonium sulfide
CC {ECO:0000269|PubMed:19419967};
CC Vmax=1.4 umol/sec/mg enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:19419967};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0WP12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WP12-2; Sequence=VSP_059984;
CC Name=3;
CC IsoId=Q0WP12-3; Sequence=VSP_038905;
CC -!- TISSUE SPECIFICITY: Expressed in shoots, leaves, stems, inflorescences,
CC flowers and green siliques. {ECO:0000269|PubMed:14561407}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Increased sensitivity to thiocyanate in medium and lower
CC methyl halide emissions. {ECO:0000269|PubMed:14561407,
CC ECO:0000269|PubMed:19419967}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TPMT family. {ECO:0000255|PROSITE-ProRule:PRU00918}.
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DR EMBL; AC004005; AAC23400.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10343.1; -; Genomic_DNA.
DR EMBL; AY044314; AAK73255.1; -; mRNA.
DR EMBL; AY086360; AAM64428.1; -; mRNA.
DR EMBL; AK229273; BAF01137.1; -; mRNA.
DR EMBL; AK319169; BAH57284.1; -; mRNA.
DR PIR; T00671; T00671.
DR RefSeq; NP_181919.1; NM_129953.3. [Q0WP12-1]
DR PDB; 3LCC; X-ray; 1.80 A; A=1-227.
DR PDBsum; 3LCC; -.
DR AlphaFoldDB; Q0WP12; -.
DR SMR; Q0WP12; -.
DR STRING; 3702.AT2G43910.2; -.
DR iPTMnet; Q0WP12; -.
DR PaxDb; Q0WP12; -.
DR PRIDE; Q0WP12; -.
DR ProteomicsDB; 230214; -. [Q0WP12-1]
DR DNASU; 818995; -.
DR EnsemblPlants; AT2G43910.1; AT2G43910.1; AT2G43910. [Q0WP12-1]
DR GeneID; 818995; -.
DR Gramene; AT2G43910.1; AT2G43910.1; AT2G43910. [Q0WP12-1]
DR KEGG; ath:AT2G43910; -.
DR Araport; AT2G43910; -.
DR TAIR; locus:2051728; AT2G43910.
DR eggNOG; ENOG502QS1V; Eukaryota.
DR InParanoid; Q0WP12; -.
DR OMA; KEREMTW; -.
DR PhylomeDB; Q0WP12; -.
DR BRENDA; 2.1.1.165; 399.
DR BRENDA; 2.1.1.9; 399.
DR EvolutionaryTrace; Q0WP12; -.
DR PRO; PR:Q0WP12; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WP12; baseline and differential.
DR Genevisible; Q0WP12; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0102215; F:thiocyanate methyltransferase activity; IEA:RHEA.
DR GO; GO:0018708; F:thiol S-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IMP:UniProtKB.
DR GO; GO:0019762; P:glucosinolate catabolic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR044995; TMT/HOL.
DR InterPro; IPR008854; TPMT.
DR PANTHER; PTHR32183; PTHR32183; 1.
DR Pfam; PF05724; TPMT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51585; SAM_MT_TPMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..227
FT /note="Thiocyanate methyltransferase 1"
FT /id="PRO_0000393277"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20376845,
FT ECO:0007744|PDB:3LCC"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00918,
FT ECO:0000269|PubMed:20376845, ECO:0007744|PDB:3LCC"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20376845,
FT ECO:0007744|PDB:3LCC"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20376845,
FT ECO:0007744|PDB:3LCC"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00918,
FT ECO:0000269|PubMed:20376845, ECO:0007744|PDB:3LCC"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20376845,
FT ECO:0007744|PDB:3LCC"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:20376845,
FT ECO:0007744|PDB:3LCC"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_038905"
FT VAR_SEQ 215..227
FT /note="KGKEKLGRWKKIN -> QREAGKVEEDQLIPKKEILLFGKSVICVIYKE
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_059984"
FT HELIX 20..41
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3LCC"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:3LCC"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3LCC"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:3LCC"
FT TURN 212..216
FT /evidence="ECO:0007829|PDB:3LCC"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:3LCC"
SQ SEQUENCE 227 AA; 25289 MW; 84EBDE8BC0EC46BB CRC64;
MAEEQQNSDQ SNGGNVIPTP EEVATFLHKT VEEGGWEKCW EEEITPWDQG RATPLIVHLV
DTSSLPLGRA LVPGCGGGHD VVAMASPERF VVGLDISESA LAKANETYGS SPKAEYFSFV
KEDVFTWRPT ELFDLIFDYV FFCAIEPEMR PAWAKSMYEL LKPDGELITL MYPITDHVGG
PPYKVDVSTF EEVLVPIGFK AVSVEENPHA IPTRKGKEKL GRWKKIN
