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P23686 (METK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
S-adenosylmethionine synthase 1

Short name=AdoMet synthase 1
EC=2.5.1.6
Alternative name(s):
Methionine adenosyltransferase 1
Short name=MAT 1
Gene names
Name:SAM1
Ordered Locus Names:At1g02500
ORF Names:T14P4.17, T14P4_22
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme By similarity.

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

Cofactor

Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.

Binds 1 potassium ion per subunit By similarity.

Enzyme regulation

Reversibly inhibited by NO. Repressed by 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) and N-ethylmaleimide (NEM). Ref.8

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in stems and roots. Ref.7

Post-translational modification

S-nitrosylated in the presence of NO. The inhibition of SAM1 activity by S-nitrosylation could contribute to the cross-talk between ethylene and NO signaling.

Ubiquitinated. Ref.9

Sequence similarities

Belongs to the AdoMet synthase family.

Sequence caution

The sequence AAK96504.1 differs from that shown. Reason: Frameshift at position 75.

The sequence AAL31222.1 differs from that shown. Reason: Frameshift at position 75.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393S-adenosylmethionine synthase 1
PRO_0000174456

Regions

Nucleotide binding119 – 1246ATP Potential
Nucleotide binding267 – 2748ATP Potential

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2711Potassium By similarity
Metal binding2791Magnesium By similarity
Binding site1471ATP Potential

Amino acid modifications

Modified residue1141S-nitrosocysteine

Experimental info

Mutagenesis1141C → R: Loss of the NO-mediated inhibition by S-nitrosylation. Ref.8
Sequence conflict1171E → D in AAA32868. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23686 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 27B0AF8AF55D2FF3

FASTA39343,158
        10         20         30         40         50         60 
METFLFTSES VNEGHPDKLC DQISDAVLDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK 

        70         80         90        100        110        120 
ATVDYEKIVR DTCRAIGFVS DDVGLDADKC KVLVNIEQQS PDIAQGVHGH FTKCPEEIGA 

       130        140        150        160        170        180 
GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CAWLRPDGKT QVTVEYYNDK 

       190        200        210        220        230        240 
GAMVPIRVHT VLISTQHDET VTNDEIARDL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI 

       250        260        270        280        290        300 
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSVVANGMAR 

       310        320        330        340        350        360 
RALVQVSYAI GVPEPLSVFV DTYETGLIPD KEILKIVKES FDFRPGMMTI NLDLKRGGNG 

       370        380        390 
RFLKTAAYGH FGRDDPDFTW EVVKPLKWDK PQA 

« Hide

References

« Hide 'large scale' references
[1]"Strong cellular preference in the expression of a housekeeping gene of Arabidopsis thaliana encoding S-adenosylmethionine synthetase."
Peleman J., Boerjan W., Engler G., Seurinck J., Botterman J., Alliotte T., van Montagu M., Inze D.
Plant Cell 1:81-93(1989) [PubMed: 2535470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana."
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R. expand/collapse author list , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.
Plant J. 4:1051-1061(1993) [PubMed: 8281187] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116 AND 363-393.
Strain: cv. Columbia.
Tissue: Green siliques.
[7]"Structure and expression analyses of the S-adenosylmethionine synthetase gene family in Arabidopsis thaliana."
Peleman J., Saito K., Cottyn B., Engler G., Seurinck J., van Montagu M., Inze D.
Gene 84:359-369(1989) [PubMed: 2482229] [Abstract]
Cited for: TISSUE SPECIFICITY.
Strain: cv. Columbia.
[8]"Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation."
Lindermayr C., Saalbach G., Bahnweg G., Durner J.
J. Biol. Chem. 281:4285-4291(2006) [PubMed: 16365035] [Abstract]
Cited for: S-NITROSYLATION, MUTAGENESIS OF CYS-114, ENZYME REGULATION.
[9]"Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
Plant J. 59:344-358(2009) [PubMed: 19292762] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55077 Genomic DNA. Translation: AAA32868.1.
AC022521 Genomic DNA. Translation: AAG10639.1.
CP002684 Genomic DNA. Translation: AEE27437.1.
CP002684 Genomic DNA. Translation: AEE27438.1.
AF325061 mRNA. Translation: AAG40413.1.
AY092955 mRNA. Translation: AAM12954.1.
AF428440 mRNA. Translation: AAL16209.1.
AY052311 mRNA. Translation: AAK96504.1. Frameshift.
AY061895 mRNA. Translation: AAL31222.1. Frameshift.
AY087703 mRNA. Translation: AAM65240.1.
Z17672 mRNA. Translation: CAA79031.1.
Z17762 mRNA. Translation: CAA79057.1.
IPIIPI00545903.
PIRC86155.
JN0131.
RefSeqNP_171751.1. NM_100131.2.
NP_849577.1. NM_179246.1.
UniGeneAt.24731.
At.72241.

3D structure databases

ProteinModelPortalP23686.
SMRP23686. Positions 3-388.
ModBaseSearch...

Protein-protein interaction databases

STRINGP23686.

2D gel databases

SWISS-2DPAGEP99056.

Proteomic databases

PRIDEP23686.
ProMEXP23686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G02500.1; AT1G02500.1; AT1G02500.
AT1G02500.2; AT1G02500.2; AT1G02500.
GeneID839501.
GenomeReviewsGene locus AT1G02500 in contig CT485782_GR.
KEGGath:AT1G02500.
NMPDRfig|3702.1.peg.370.

Organism-specific databases

TAIRAt1g02500.

Phylogenomic databases

eggNOGKOG1506.
GeneTreeEPGT00050000019410.
HOGENOMHBG443662.
InParanoidP23686.
OMASTKGFDY.
PhylomeDBP23686.
ProtClustDBPLN02243.

Enzyme and pathway databases

BioCycARA:AT1G02500-MONOMER.
MetaCyc:AT1G02500-MONOMER.

Gene expression databases

ArrayExpressP23686.
GenevestigatorP23686.
GermOnlineAT1G02500. Arabidopsis thaliana.

Family and domain databases

InterProIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
KOK00789.
PANTHERPTHR11964. S-AdoMet_synt. 1 hit.
PfamPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000497. MAT. 1 hit.
SUPFAMSSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMsTIGR01034. MetK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK1_ARATH
AccessionPrimary (citable) accession number: P23686
Secondary accession number(s): Q941A8, Q9FEE0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: June 20, 2002
Last modified: November 16, 2011
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families