HMT2_ARATH
ID HMT2_ARATH Reviewed; 333 AA.
AC Q9M1W4; Q0WTD0; Q9SDL6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Homocysteine S-methyltransferase 2;
DE EC=2.1.1.10;
DE AltName: Full=S-methylmethionine:homocysteine methyltransferase 2;
DE Short=AtHMT-2;
DE Short=SMM:Hcy S-methyltransferase 2;
GN Name=HMT-2; OrderedLocusNames=At3g63250; ORFNames=F16M2.100;
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 [GENOMIC DNA], ENZYME ACTIVITY, AND SUBUNIT.
RX PubMed=10747987; DOI=10.1074/jbc.m001116200;
RA Ranocha P., Bourgis F., Ziemak M.J., Rhodes D., Gage D.A., Hanson A.D.;
RT "Characterization and functional expression of cDNAs encoding methionine-
RT sensitive and -insensitive homocysteine S-methyltransferases from
RT Arabidopsis.";
RL J. Biol. Chem. 275:15962-15968(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [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., 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 [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROBABLE FUNCTION OF SMM CYCLE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=11309147; DOI=10.1046/j.1365-313x.2001.00988.x;
RA Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., Hanson A.D.;
RT "The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and
RT activity.";
RL Plant J. 25:575-584(2001).
CC -!- FUNCTION: Catalyzes methyl transfer from S-methylmethionine (SMM) to
CC adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and
CC HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants,
CC which is probably required to achieve short term control of AdoMet
CC level.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + S-methyl-L-methionine = H(+) + 2 L-
CC methionine; Xref=Rhea:RHEA:26337, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58199, ChEBI:CHEBI:58252; EC=2.1.1.10;
CC Evidence={ECO:0000269|PubMed:10747987};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00333};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for S-methylmethionine {ECO:0000269|PubMed:11309147};
CC KM=225 uM for (S,S)-AdoMet {ECO:0000269|PubMed:11309147};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10747987}.
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=Q9M1W4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in roots. Expressed in
CC rosette leaves, cauline leaves and developing seeds.
CC {ECO:0000269|PubMed:11309147}.
CC -!- MISCELLANEOUS: In contrast to HMT-1, it is not inhibited by methionine.
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DR EMBL; AF219223; AAF23822.1; -; Genomic_DNA.
DR EMBL; AL138648; CAB86426.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80456.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63398.1; -; Genomic_DNA.
DR EMBL; AF428402; AAL16170.1; -; mRNA.
DR EMBL; BT010165; AAQ22634.1; -; mRNA.
DR EMBL; AK227627; BAE99618.1; -; mRNA.
DR PIR; T48114; T48114.
DR PIR; T51939; T51939.
DR RefSeq; NP_001319825.1; NM_001340195.1. [Q9M1W4-1]
DR RefSeq; NP_191884.1; NM_116190.5. [Q9M1W4-1]
DR AlphaFoldDB; Q9M1W4; -.
DR SMR; Q9M1W4; -.
DR STRING; 3702.AT3G63250.1; -.
DR PaxDb; Q9M1W4; -.
DR PRIDE; Q9M1W4; -.
DR ProteomicsDB; 228807; -. [Q9M1W4-1]
DR DNASU; 825500; -.
DR EnsemblPlants; AT3G63250.1; AT3G63250.1; AT3G63250. [Q9M1W4-1]
DR EnsemblPlants; AT3G63250.3; AT3G63250.3; AT3G63250. [Q9M1W4-1]
DR GeneID; 825500; -.
DR Gramene; AT3G63250.1; AT3G63250.1; AT3G63250. [Q9M1W4-1]
DR Gramene; AT3G63250.3; AT3G63250.3; AT3G63250. [Q9M1W4-1]
DR KEGG; ath:AT3G63250; -.
DR Araport; AT3G63250; -.
DR TAIR; locus:2077234; AT3G63250.
DR eggNOG; KOG1579; Eukaryota.
DR HOGENOM; CLU_004914_3_2_1; -.
DR InParanoid; Q9M1W4; -.
DR OMA; AQEDYKM; -.
DR OrthoDB; 731388at2759; -.
DR PhylomeDB; Q9M1W4; -.
DR BioCyc; ARA:AT3G63250-MON; -.
DR BioCyc; MetaCyc:AT3G63250-MON; -.
DR BRENDA; 2.1.1.10; 399.
DR SABIO-RK; Q9M1W4; -.
DR PRO; PR:Q9M1W4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1W4; baseline and differential.
DR Genevisible; Q9M1W4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0047150; F:betaine-homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IDA:TAIR.
DR GO; GO:0061627; F:S-methylmethionine-homocysteine S-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0033528; P:S-methylmethionine cycle; IMP:TAIR.
DR Gene3D; 3.20.20.330; -; 1.
DR InterPro; IPR017226; Betaine-hCys_S-MeTrfase_BHMT.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PIRSF; PIRSF037505; Betaine_HMT; 1.
DR SUPFAM; SSF82282; SSF82282; 1.
DR PROSITE; PS50970; HCY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..333
FT /note="Homocysteine S-methyltransferase 2"
FT /id="PRO_0000114612"
FT DOMAIN 8..327
FT /note="Hcy-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00333"
FT CONFLICT 103
FT /note="T -> C (in Ref. 1; AAF23822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36451 MW; CB44D8F3BAC15D85 CRC64;
MTGNSFNSMK DFLKQTGGYA VIDGGLATEF ERHGADLNDP LWSAKCLVTS PHLIHTVHLD
YLEAGADIIS SASYQATIQG FEAKGFSREE SESLLKKSVE IATEARNSYY DKCGTSSSMD
DKILKKRPIL VAASVGSYGA YLADGSEYSG IYGDSITLEK LKDFHRRRLQ VLAESGADLI
AFETIPNKIE AQAFADLLEE GDVKIPGWFS FNSKDGVNVV SGDSIKECIS IAENCEKVVA
VGINCTPPRF IEGLVLEIEK VTSKPILVYP NSGESYDADR KEWVENTGVG DEDFVSYVEK
WMDAGVSLLG GCCRTTPTTI RAIHKRLVNR RSL
