HOL2_ARATH
ID HOL2_ARATH Reviewed; 227 AA.
AC O80562; B3H663;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable thiol methyltransferase 1;
DE EC=2.1.1.9;
DE AltName: Full=Protein HARMLESS TO OZONE LAYER 2;
DE Short=AtHOL2;
GN Name=HOL2; OrderedLocusNames=At2g43920; ORFNames=F6E13.5;
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 3).
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 Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP 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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase. Involved
CC in glucosinolate metabolism and defense against phytopathogens (By
CC similarity). {ECO:0000250, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a thiol + S-adenosyl-L-methionine = a methyl thioether + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:18277, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29256, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:86315; EC=2.1.1.9;
CC Evidence={ECO:0000269|PubMed:19419967};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for KSCN {ECO:0000269|PubMed:19419967};
CC KM=36 mM for KCL {ECO:0000269|PubMed:19419967};
CC KM=1.1 mM for ammonium sulfide {ECO:0000269|PubMed:19419967};
CC KM=49 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19419967};
CC Vmax=260 nmol/sec/mg enzyme toward KSCN
CC {ECO:0000269|PubMed:19419967};
CC Vmax=200 nmol/sec/mg enzyme toward KCL {ECO:0000269|PubMed:19419967};
CC Vmax=520 nmol/sec/mg enzyme toward ammonium sulfide
CC {ECO:0000269|PubMed:19419967};
CC Vmax=200 nmol/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=O80562-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80562-2; Sequence=VSP_038908, VSP_038909;
CC Name=3;
CC IsoId=O80562-3; Sequence=VSP_038910;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {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; AAC23401.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10346.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10347.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10348.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63282.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63283.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63284.1; -; Genomic_DNA.
DR EMBL; AY070741; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT012597; AAT06416.1; -; mRNA.
DR EMBL; BT014828; AAT41811.1; -; mRNA.
DR PIR; T00672; T00672.
DR RefSeq; NP_001118521.1; NM_001125049.1. [O80562-2]
DR RefSeq; NP_001154578.1; NM_001161106.2. [O80562-3]
DR RefSeq; NP_001318421.1; NM_001337066.1. [O80562-3]
DR RefSeq; NP_001325381.1; NM_001337068.1. [O80562-3]
DR RefSeq; NP_001325382.1; NM_001337067.1. [O80562-3]
DR RefSeq; NP_181920.1; NM_129954.4. [O80562-1]
DR AlphaFoldDB; O80562; -.
DR SMR; O80562; -.
DR STRING; 3702.AT2G43920.1; -.
DR iPTMnet; O80562; -.
DR PaxDb; O80562; -.
DR PRIDE; O80562; -.
DR ProteomicsDB; 230215; -. [O80562-1]
DR EnsemblPlants; AT2G43920.1; AT2G43920.1; AT2G43920. [O80562-1]
DR EnsemblPlants; AT2G43920.2; AT2G43920.2; AT2G43920. [O80562-2]
DR EnsemblPlants; AT2G43920.3; AT2G43920.3; AT2G43920. [O80562-3]
DR EnsemblPlants; AT2G43920.4; AT2G43920.4; AT2G43920. [O80562-3]
DR EnsemblPlants; AT2G43920.5; AT2G43920.5; AT2G43920. [O80562-3]
DR EnsemblPlants; AT2G43920.6; AT2G43920.6; AT2G43920. [O80562-3]
DR GeneID; 818996; -.
DR Gramene; AT2G43920.1; AT2G43920.1; AT2G43920. [O80562-1]
DR Gramene; AT2G43920.2; AT2G43920.2; AT2G43920. [O80562-2]
DR Gramene; AT2G43920.3; AT2G43920.3; AT2G43920. [O80562-3]
DR Gramene; AT2G43920.4; AT2G43920.4; AT2G43920. [O80562-3]
DR Gramene; AT2G43920.5; AT2G43920.5; AT2G43920. [O80562-3]
DR Gramene; AT2G43920.6; AT2G43920.6; AT2G43920. [O80562-3]
DR KEGG; ath:AT2G43920; -.
DR Araport; AT2G43920; -.
DR TAIR; locus:2051784; AT2G43920.
DR eggNOG; ENOG502QS1V; Eukaryota.
DR InParanoid; O80562; -.
DR OMA; CADFFTW; -.
DR PhylomeDB; O80562; -.
DR BRENDA; 2.1.1.165; 399.
DR PRO; PR:O80562; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80562; baseline and differential.
DR Genevisible; O80562; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0018708; F:thiol S-methyltransferase activity; 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; 2.
DR Pfam; PF05724; TPMT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51585; SAM_MT_TPMT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..227
FT /note="Probable thiol methyltransferase 1"
FT /id="PRO_0000393278"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12,
FT ECO:0000255|PROSITE-ProRule:PRU00918"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12,
FT ECO:0000255|PROSITE-ProRule:PRU00918"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038910"
FT VAR_SEQ 191..200
FT /note="EDVLVPVGFK -> LRRCVGSGRI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038908"
FT VAR_SEQ 201..227
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038909"
SQ SEQUENCE 227 AA; 25126 MW; 3B6F4DDC281E3B3A CRC64;
MAEEQQNSSY SIGGNILPTP EEAATFQPQV VAEGGWDKCW EDGVTPWDQG RATPLILHLL
DSSALPLGRT LVPGCGGGHD VVAMASPERF VVGLDISDKA LNKANETYGS SPKAEYFSFV
KEDVFTWRPN ELFDLIFDYV FFCAIEPEMR PAWGKSMHEL LKPDGELITL MYPMTDHEGG
APYKVALSSY EDVLVPVGFK AVSVEENPDS IPTRKGKEKL ARWKKIN
