METE2_ARATH
ID METE2_ARATH Reviewed; 765 AA.
AC Q9SRV5; Q94BN4;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2;
DE EC=2.1.1.14;
DE AltName: Full=Cobalamin-independent methionine synthase 2;
DE Short=AtMS2;
GN Name=MS2; OrderedLocusNames=At3g03780; ORFNames=F20H23.19;
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 [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15024005; DOI=10.1074/jbc.m313250200;
RA Ravanel S., Block M.A., Rippert P., Jabrin S., Curien G., Rebeille F.,
RA Douce R.;
RT "Methionine metabolism in plants: chloroplasts are autonomous for de novo
RT methionine synthesis and can import S-adenosylmethionine from the
RT cytosol.";
RL J. Biol. Chem. 279:22548-22557(2004).
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].
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.
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC methyltetrahydrofolate to homocysteine resulting in methionine
CC formation. {ECO:0000269|PubMed:15024005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC ChEBI:CHEBI:58207; EC=2.1.1.14;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for 5-methyltetrahydrofolate {ECO:0000269|PubMed:15024005};
CC Vmax=20.7 nmol/min/mg enzyme toward 5-methyltetrahydrofolate
CC {ECO:0000269|PubMed:15024005};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15024005}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and siliques.
CC {ECO:0000269|PubMed:15024005}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC family. {ECO:0000305}.
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DR EMBL; AJ608674; CAE55864.1; -; mRNA.
DR EMBL; AC009540; AAF00639.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73989.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73990.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73991.1; -; Genomic_DNA.
DR EMBL; AY040010; AAK64167.1; -; mRNA.
DR EMBL; AY150385; AAN12930.1; -; mRNA.
DR EMBL; AY084559; AAM61126.1; -; mRNA.
DR RefSeq; NP_001118564.1; NM_001125092.1.
DR RefSeq; NP_187028.1; NM_111249.5.
DR RefSeq; NP_850507.1; NM_180176.4.
DR AlphaFoldDB; Q9SRV5; -.
DR SMR; Q9SRV5; -.
DR BioGRID; 6480; 7.
DR IntAct; Q9SRV5; 1.
DR MINT; Q9SRV5; -.
DR STRING; 3702.AT3G03780.1; -.
DR iPTMnet; Q9SRV5; -.
DR MetOSite; Q9SRV5; -.
DR PaxDb; Q9SRV5; -.
DR PRIDE; Q9SRV5; -.
DR ProteomicsDB; 232235; -.
DR DNASU; 821147; -.
DR EnsemblPlants; AT3G03780.1; AT3G03780.1; AT3G03780.
DR EnsemblPlants; AT3G03780.2; AT3G03780.2; AT3G03780.
DR EnsemblPlants; AT3G03780.3; AT3G03780.3; AT3G03780.
DR GeneID; 821147; -.
DR Gramene; AT3G03780.1; AT3G03780.1; AT3G03780.
DR Gramene; AT3G03780.2; AT3G03780.2; AT3G03780.
DR Gramene; AT3G03780.3; AT3G03780.3; AT3G03780.
DR KEGG; ath:AT3G03780; -.
DR Araport; AT3G03780; -.
DR TAIR; locus:2079434; AT3G03780.
DR eggNOG; KOG2263; Eukaryota.
DR HOGENOM; CLU_013175_0_0_1; -.
DR InParanoid; Q9SRV5; -.
DR OMA; NDILPWI; -.
DR OrthoDB; 237390at2759; -.
DR PhylomeDB; Q9SRV5; -.
DR BioCyc; ARA:AT3G03780-MON; -.
DR BioCyc; MetaCyc:AT3G03780-MON; -.
DR SABIO-RK; Q9SRV5; -.
DR UniPathway; UPA00051; UER00082.
DR PRO; PR:Q9SRV5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRV5; baseline and differential.
DR Genevisible; Q9SRV5; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008705; F:methionine synthase activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IMP:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd03311; CIMS_C_terminal_like; 1.
DR Gene3D; 3.20.20.210; -; 2.
DR HAMAP; MF_00172; Meth_synth; 1.
DR InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR InterPro; IPR006276; Cobalamin-indep_Met_synthase.
DR InterPro; IPR002629; Met_Synth_C/arc.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cytoplasm; Metal-binding; Methionine biosynthesis;
KW Methyltransferase; Reference proteome; Transferase; Zinc.
FT CHAIN 1..765
FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine
FT methyltransferase 2"
FT /id="PRO_0000424356"
FT ACT_SITE 701
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 18
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 116
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 437..439
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 437..439
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 490
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 490
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 495
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 518
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 521..522
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 567
FT /ligand="5-methyltetrahydropteroyltri-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58207"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 605
FT /ligand="L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:58199"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 605
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 658
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P82610"
FT BINDING 733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O50008"
FT CONFLICT 763
FT /note="S -> N (in Ref. 4; AAK64167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 84584 MW; EB478D815910E701 CRC64;
MASHIVGYPR MGPKRELKFA LESFWDGKSS ADDLQKVSAD LRSDIWKQMS AAGIKYIPSN
TFSHYDQVLD TTAMLGAVPS RYGFTSGEIG LDVYFSMARG NASVPAMEMT KWFDTNYHYI
VPELGPEVKF SYASHKAVNE YKEAKALGVE TVPVLVGPVS YLLLSKLAKG VDKSFDLLSL
LPKILPVYKE VIAELKAAGA SWIQLDEPLF VMDLEGHKLQ AFSGAYAELE STLSGLNVLV
ETYFADIPAE AYKTLTSLKG VTAFGFDLVR GTKTIDLIKS GFPQGKYLFA GVVDGRNIWA
NDLAASLITL QSLEGVVGKD KLVVSTSCSL LHTAVDLINE TKLDAEIKSW LAFAAQKVVE
VDALAKALAG QTNESFFTAN ADALSSRRSS PRVTNESVQK AAAALKGSDH RRTTEVSARL
DAQQKKLNLP ILPTTTIGSF PQTVELRRVR REYKAKKISE EDYVKAIKEE IKKVVDIQED
LDIDVLVHGE PERNDMVEYF GEQLSGFAFT ANGWVQSYGS RCVKPPVIYG DVSRPKPMTV
FWSSTAQSMT KRPMKGMLTG PVTILNWSFV RNDQPRHETC YQIALAIKDE VEDLEKGGIG
VIQIDEAALR EGLPLRKAEH SFYLDWAVHS FRITNCGVQD STQIHTHMCY SNFNDIIHSI
IDMDADVITI ENSRSDEKLL SVFREGVKYG AGIGPGVYDI HSPRIPSTDE IADRINKMLA
VLEQNILWVN PDCGLKTRKY TEVKPALKAM VDAAKLIRSQ LGSAK
