HOL3_ARATH
ID HOL3_ARATH Reviewed; 226 AA.
AC Q6AWU6; O80564;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable thiol methyltransferase 2;
DE EC=2.1.1.9;
DE AltName: Full=Protein HARMLESS TO OZONE LAYER 3;
DE Short=AtHOL3;
GN Name=HOL3; OrderedLocusNames=At2g43940; ORFNames=F6E13.7;
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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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.
CC {ECO:0000269|Ref.4}.
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=3.1 mM for KSCN {ECO:0000269|PubMed:19419967};
CC KM=1.3 mM for ammonium sulfide {ECO:0000269|PubMed:19419967};
CC KM=40 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:19419967};
CC Vmax=110 nmol/sec/mg enzyme toward KSCN
CC {ECO:0000269|PubMed:19419967};
CC Vmax=1.3 umol/sec/mg enzyme toward ammonium sulfide
CC {ECO:0000269|PubMed:19419967};
CC Vmax=410 nmol/sec/mg enzyme toward S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:19419967};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23402.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004005; AAC23402.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10350.1; -; Genomic_DNA.
DR EMBL; BT015152; AAT85748.1; -; mRNA.
DR EMBL; BT015729; AAU45227.1; -; mRNA.
DR PIR; T00674; T00674.
DR RefSeq; NP_850403.1; NM_180072.3.
DR AlphaFoldDB; Q6AWU6; -.
DR SMR; Q6AWU6; -.
DR STRING; 3702.AT2G43940.1; -.
DR iPTMnet; Q6AWU6; -.
DR PaxDb; Q6AWU6; -.
DR PRIDE; Q6AWU6; -.
DR ProteomicsDB; 230216; -.
DR DNASU; 818998; -.
DR EnsemblPlants; AT2G43940.1; AT2G43940.1; AT2G43940.
DR GeneID; 818998; -.
DR Gramene; AT2G43940.1; AT2G43940.1; AT2G43940.
DR KEGG; ath:AT2G43940; -.
DR Araport; AT2G43940; -.
DR TAIR; locus:2051824; AT2G43940.
DR eggNOG; ENOG502QS1V; Eukaryota.
DR HOGENOM; CLU_056435_1_1_1; -.
DR InParanoid; Q6AWU6; -.
DR OMA; RWAALWD; -.
DR OrthoDB; 1590477at2759; -.
DR PhylomeDB; Q6AWU6; -.
DR BRENDA; 2.1.1.165; 399.
DR PRO; PR:Q6AWU6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6AWU6; baseline and differential.
DR Genevisible; Q6AWU6; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA: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; 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 Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..226
FT /note="Probable thiol methyltransferase 2"
FT /id="PRO_0000393279"
FT BINDING 29
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 33
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 40
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 88
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 116..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0WP12"
SQ SEQUENCE 226 AA; 25043 MW; 5A85036E5E51FDAD CRC64;
MENAGKATSL QSSRDLFHRL MSENSSGGWE KSWEAGATPW DLGKPTPVIA HLVETGSLPN
GRALVPGCGT GYDVVAMASP DRHVVGLDIS KTAVERSTKK FSTLPNAKYF SFLSEDFFTW
EPAEKFDLIF DYTFFCAFEP GVRPLWAQRM EKLLKPGGEL ITLMFPIDER SGGPPYEVSV
SEYEKVLIPL GFEAISIVDN ELAVGPRKGM EKLGRWKKSS TFHSTL
