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UniProtKB/Swiss-Prot entry Q9M1W4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HMT2_ARATH
Primary accession number Q9M1W4
Secondary accession number Q9SDL6
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 35)
Name and origin of the protein
Protein name Homocysteine S-methyltransferase 2
Synonyms EC 2.1.1.10
S-methylmethionine:homocysteine methyltransferase 2
SMM:Hcy S-methyltransferase 2
AtHMT-2
Gene name
Name: HMT-2
OrderedLocusNames: At3g63250
ORFNames: F16M2.100
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME ACTIVITY, AND SUBUNIT.
DOI=10.1074/jbc.M001116200; PubMed=10747987 [NCBI, ExPASy, EBI, Israel, Japan]
Ranocha P., Bourgis F., Ziemak M.J., Rhodes D., Gage D.A., Hanson A.D.;
"Characterization and functional expression of cDNAs encoding methionine-sensitive and -insensitive homocysteine S-methyltransferases from Arabidopsis.";
J. Biol. Chem. 275:15962-15968(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
PROBABLE FUNCTION OF SMM CYCLE, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=11309147 [NCBI, ExPASy, EBI, Israel, Japan]
Ranocha P., McNeil S.D., Ziemak M.J., Li C., Tarczynski M.C., Hanson A.D.;
"The S-methylmethionine cycle in angiosperms: ubiquity, antiquity and activity.";
Plant J. 25:575-584(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF219223; AAF23822.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138648; CAB86426.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF428402; AAL16170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT010165; AAQ22634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48114; T48114.
T51939; T51939.
RefSeq NP_191884.1; -.
UniGene At.21554
3D structure databases
ModBase Q9M1W4.
Organism-specific databases
TAIR At3g63250; -.
Gene expression databases
ArrayExpress Q9M1W4; -.
Ontologies
GO
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009086; Biological process: methionine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003726; S_MeTrfase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.330; S_methyl_trans; 1.
Pfam PF02574; S-methyl_trans; 1.
Pfam graphical view of domain structure.
PROSITE PS50970; HCY; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9M1W4.
ProtoNet Q9M1W4.
Genome annotation databases
GeneID 825500; -.
GenomeReviews BA000014_GR; AT3G63250.
KEGG ath:AT3G63250; -.
NMPDR fig|3702.1.peg.17715; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Amino-acid biosynthesis; Complete proteome; Metal-binding; Methionine biosynthesis; Methyltransferase; S-adenosyl-L-methionine; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   333  333     Homocysteine S-methyltransferase 2. PRO_0000114612
DOMAIN   8   327  320     Hcy-binding. 
METAL   245   245        Zinc (Potential). 
METAL   312   312        Zinc (Potential). 
METAL   313   313        Zinc (Potential). 
CONFLICT   103   103        T -> C (in Ref. 1; AAF23822). 
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 36451 Da [This is the MW of the unprocessed precursor] CRC64: CB44D8F3BAC15D85 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTGNSFNSMK DFLKQTGGYA VIDGGLATEF ERHGADLNDP LWSAKCLVTS PHLIHTVHLD 

        70         80         90        100        110        120 
YLEAGADIIS SASYQATIQG FEAKGFSREE SESLLKKSVE IATEARNSYY DKCGTSSSMD 

       130        140        150        160        170        180 
DKILKKRPIL VAASVGSYGA YLADGSEYSG IYGDSITLEK LKDFHRRRLQ VLAESGADLI 

       190        200        210        220        230        240 
AFETIPNKIE AQAFADLLEE GDVKIPGWFS FNSKDGVNVV SGDSIKECIS IAENCEKVVA 

       250        260        270        280        290        300 
VGINCTPPRF IEGLVLEIEK VTSKPILVYP NSGESYDADR KEWVENTGVG DEDFVSYVEK 

       310        320        330 
WMDAGVSLLG GCCRTTPTTI RAIHKRLVNR RSL 

Q9M1W4 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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