P13444 (METK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase isoform type-1
Short name=AdoMet synthase 1
EC=2.5.1.6

Alternative name(s):
Methionine adenosyltransferase 1
Short name=MAT 1
Methionine adenosyltransferase I/III
Short name=MAT-I/III

Gene names

Name:	Mat1a
Synonyms:	Ams1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
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.
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subunit structure	Homotetramer (MAT-I) or homodimer (MAT-III).
Tissue specificity	Expressed in liver. Ref.1
Post-translational modification	S-nitrosylation of Cys-121 inactivates the enzyme.
Sequence similarities	Belongs to the AdoMet synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
PTM	Disulfide bond S-nitrosylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Inferred from direct assay. Source: RGD one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein homotetramerization Inferred from direct assay. Source: RGD
Molecular function	ADP binding Inferred from direct assay Ref.7. Source: RGD ATP binding Inferred from direct assay Ref.7. Source: RGD amino acid binding Inferred from direct assay Ref.7. Source: RGD magnesium ion binding Inferred from direct assay Ref.7. Source: RGD methionine adenosyltransferase activity Inferred from direct assay. Source: RGD protein homodimerization activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-961260,EBI-961260

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 397

397

S-adenosylmethionine synthase isoform type-1

PRO_0000174434

Regions

Nucleotide binding

132 – 137

6

ATP Potential

Sites

Metal binding

32

1

Magnesium By similarity

Metal binding

58

1

Potassium By similarity

Metal binding

284

1

Potassium By similarity

Metal binding

292

1

Magnesium By similarity

Binding site

30

1

Substrate By similarity

Binding site

160

1

ATP Potential

Binding site

180

1

Substrate By similarity

Binding site

248

1

Substrate By similarity

Binding site

250

1

Substrate; via carbonyl oxygen By similarity

Binding site

259

1

Substrate By similarity

Amino acid modifications

Modified residue

121

1

S-nitrosocysteine Ref.5

Disulfide bond

35 ↔ 61

Ref.6

Experimental info

Sequence conflict

345

1

Missing in AAH89770. Ref.3

Secondary structure

1

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397

Helix Strand Turn

Details...

Beta strand

19 – 26

8

Helix

31 – 47

17

Beta strand

56 – 61

6

Beta strand

63 – 73

11

Helix

80 – 91

12

Turn

96 – 99

4

Turn

102 – 104

3

Beta strand

105 – 109

5

Beta strand

137 – 144

8

Helix

153 – 171

19

Beta strand

172 – 174

3

Beta strand

177 – 190

14

Beta strand

197 – 210

14

Beta strand

212 – 214

3

Helix

216 – 225

10

Turn

226 – 231

6

Turn

234 – 236

3

Beta strand

242 – 246

5

Turn

267 – 272

6

Beta strand

273 – 276

4

Helix

291 – 308

18

Beta strand

313 – 321

9

Beta strand

331 – 335

5

Turn

343 – 346

4

Helix

347 – 354

8

Helix

359 – 365

7

Turn

366 – 369

4

Helix

373 – 376

4

Beta strand

381 – 383

3

Helix

388 – 390

3

Sequences

	Sequence		Length	Mass (Da)
	P13444 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: A847A8CCBB2007BA	FASTA	397	43,698
	10 20 30 40 50 60 MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD PNAKVACETV 70 80 90 100 110 120 CKTGMVLLCG EITSMAMIDY QRVVRDTIKH IGYDDSAKGF DFKTCNVLVA LEQQSPDIAQ 130 140 150 160 170 180 CVHLDRNEED VGAGDQGLMF GYATDETEEC MPLTIVLAHK LNTRMADLRR SGVLPWLRPD 190 200 210 220 230 240 SKTQVTVQYV QDNGAVIPVR VHTIVISVQH NEDITLEAMR EALKEQVIKA VVPAKYLDED 250 260 270 280 290 300 TIYHLQPSGR FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR 310 320 330 340 350 360 WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSK KTERDELLEV VNKNFDLRPG 370 380 390 VIVRDLDLKK PIYQKTACYG HFGRSEFPWE VPKKLVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a cDNA encoding the rat liver S-adenosylmethionine synthetase." Horikawa S., Ishikawa M., Ozasa H., Tsukada K. Eur. J. Biochem. 184:497-501(1989) [PubMed: 2806235] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Wistar. Tissue: Liver.
[2]	"Analysis of the 5' non-coding region of rat liver S-adenosylmethionine synthetase mRNA and comparison of the Mr deduced from the cDNA sequence and the purified enzyme." Alvarez L., Asuncion M., Corrales F., Pajares M.A., Mato J.M. FEBS Lett. 290:142-146(1991) [PubMed: 1915866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spleen.
[4]	"Nitric oxide inactivates rat hepatic methionine adenosyltransferase In vivo by S-nitrosylation." Ruiz F., Corrales F.J., Miqueo C., Mato J.M. Hepatology 28:1051-1057(1998) [PubMed: 9755242] [Abstract] Cited for: S-NITROSYLATION.
[5]	"Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol." Perez-Mato I., Castro C., Ruiz F.A., Corrales F.J., Mato J.M. J. Biol. Chem. 274:17075-17079(1999) [PubMed: 10358060] [Abstract] Cited for: S-NITROSYLATION AT CYS-121.
[6]	"Assignment of a single disulfide bridge in rat liver methionine adenosyltransferase." Martinez-Chantar M.L., Pajares M.A. Eur. J. Biochem. 267:132-137(2000) [PubMed: 10601859] [Abstract] Cited for: DISULFIDE BOND.
[7]	"Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism." Gonzalez B., Pajares M.A., Hermoso J.A., Guillerm D., Guillerm G., Sanz-Aparicio J. J. Mol. Biol. 331:407-416(2003) [PubMed: 12888348] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X15734 mRNA. Translation: CAA33754.1.
X60822 mRNA. No translation available.
BC089770 mRNA. Translation: AAH89770.1.

IPI

IPI00201436.

PIR

S06114.

RefSeq

NP_036992.2. NM_012860.2.

UniGene

Rn.10418.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O90	X-ray	3.10	A/B	1-397	[»]
1O92	X-ray	3.19	A/B	1-397	[»]
1O93	X-ray	3.49	A/B	1-397	[»]
1O9T	X-ray	2.90	A/B	1-397	[»]
1QM4	X-ray	2.66	A/B	1-397	[»]

ProteinModelPortal

P13444.

SMR

P13444. Positions 17-397.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13444. 1 interaction.

STRING

P13444.

PTM databases

PhosphoSite

P13444.

Proteomic databases

PRIDE

P13444.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25331.

KEGG

rno:25331.

Organism-specific databases

CTD

4143.

RGD

3050. Mat1a.

Phylogenomic databases

eggNOG

maNOG13149.

HOVERGEN

HBG001562.

PhylomeDB

P13444.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-8568.

Gene expression databases

Genevestigator

P13444.

Family and domain databases

InterPro

IPR022631. 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]

KO

K00789.

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_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

606211.

Entry information

Entry name

METK1_RAT

Accession

Primary (citable) accession number: P13444
Secondary accession number(s): Q5FVU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 1, 1990
Last modified:	November 16, 2011
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program