Reviewed, UniProtKB/Swiss-Prot P23686 (METK1_ARATH)

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthetase 1
Short name=AdoMet synthetase 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7
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.6
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.
Sequence similarities	Belongs to the AdoMet synthetase 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.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
PTM	S-nitrosylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Ref.1 Traceable author statement. Source: TAIR one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	cell wall Inferred from direct assay. Source: TAIR cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Ref.7 Inferred from direct assay. Source: TAIR potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	S-adenosylmethionine synthetase 1		PRO_0000174456
Regions
	Nucleotide binding	119 – 124	6	ATP Potential
	Nucleotide binding	267 – 274	8	ATP Potential
Sites
	Metal binding	17	1	Magnesium By similarity
	Metal binding	43	1	Potassium By similarity
	Metal binding	271	1	Potassium By similarity
	Metal binding	279	1	Magnesium By similarity
	Binding site	147	1	ATP Potential
Amino acid modifications
	Modified residue	114	1	S-nitrosocysteine
Experimental info
	Mutagenesis	114	1	C → R: Loss of the NO-mediated inhibition by S-nitrosylation. Ref.7
	Sequence conflict	117	1	E → D in AAA32868. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23686-1 [UniParc]. Last modified June 20, 2002. Version 2. Checksum: 27B0AF8AF55D2FF3	FASTA	393	43,158
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. , 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.
[4]	"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].
[5]	"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. , 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.
[6]	"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.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55077 Genomic DNA. Translation: AAA32868.1. AC022521 Genomic DNA. Translation: AAG10639.1. 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.
IPI	IPI00545903.
PIR	C86155. JN0131.
RefSeq	NP_171751.1. NP_849577.1.
UniGene	At.24731 At.27897 At.72241
3D structure databases
SMR	P23686. Positions 3-388.
ModBase	Search...
Protein-protein interaction databases
STRING	P23686.
2-D gel databases
SWISS-2DPAGE	P99056.
Proteomic databases
PRIDE	P23686.
ProMEX	P23686.
Genome annotation databases
GeneID	839501.
GenomeReviews	Gene locus AT1G02500 in contig CT485782_GR.
KEGG	ath:AT1G02500.
NMPDR	fig|3702.1.peg.370.
Organism-specific databases
TAIR	At1g02500.
Phylogenomic databases
eggNOG	KOG1506.
HOGENOM	HBG443662.
InParanoid	P23686.
OMA	WIAKSIV.
PhylomeDB	P23686.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G02500-MONOMER.
BRENDA	2.5.1.6. 302.
Gene expression databases
ArrayExpress	P23686.
Genevestigator	P23686.
GermOnline	AT1G02500. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002133. S-AdoMet_synthetase. [Graphical view]
PANTHER	PTHR11964. S-AdoMet_synt. 1 hit.
Pfam	PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view]
PIRSF	PIRSF000497. MAT. 1 hit.
SUPFAM	SSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMs	TIGR01034. metK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHETASE_1. 1 hit. PS00377. ADOMET_SYNTHETASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK1_ARATH

Accession

Primary (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:	March 2, 2010
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)