P56460 (METK_HELPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
MAT
Methionine adenosyltransferase

Gene names

Name:	metK
Ordered Locus Names:	HP_0197

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. HAMAP MF_00086
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP MF_00086
Cofactor	Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity. HAMAP MF_00086
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP MF_00086
Subunit structure	Homotetramer By similarity. HAMAP MF_00086
Subcellular location	Cytoplasm HAMAP MF_00086.
Sequence similarities	Belongs to the AdoMet synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 385	385	S-adenosylmethionine synthase HAMAP MF_00086		PRO_0000174531
Regions
	Nucleotide binding	260 – 267	8	ATP Potential
Sites
	Metal binding	18	1	Magnesium By similarity
	Metal binding	44	1	Potassium By similarity
	Metal binding	264	1	Potassium By similarity
	Metal binding	272	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56460 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: B1262A82075ADB5A	FASTA	385	42,362
	10 20 30 40 50 60 MKDSFLFTSE SVTEGHPDKM ADQISDAVLD YIIERDQKAK VACETLVSNG FCMITGELKT 70 80 90 100 110 120 SVYAPMQEIA REVVKKIGYT DALYGFDYRS AAVLNGVGEQ SPDINQGVDR EDGEIGAGDQ 130 140 150 160 170 180 GLMFGYACKE TETLMPLPIH LAHQLTFALA QKRKDNTLPF LRPDGKSQVS VRYENNKPVS 190 200 210 220 230 240 IDTIVISTQH SPEVSQKHLK EAVIEEIVYK VLSKEYLHDN IKFFVNPTGK FVIGGPQGDA 250 260 270 280 290 300 GLTGRKIIVD TYGGSCPHGG GAFSGKDPSK VDRSAAYAAR YVAKNLVASG VCDKATVQLA 310 320 330 340 350 360 YAIGVIEPVS IYVNTHNTSK YSSAELEKCV KSVFKLTPKG IIESLDLLRP IYSLTSAYGH 370 380 FGRELEEFTW EKTNKAEEIK AFFKR

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD07267.1.
PIR	E64544.
RefSeq	NP_206996.1. NC_000915.1.
3D structure databases
ProteinModelPortal	P56460.
SMR	P56460. Positions 6-380.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3226N.
MINT	MINT-177108.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	898926.
GenomeReviews	Gene locus HP_0197 in contig AE000511_GR.
KEGG	hpy:HP0197.
NMPDR	fig|85962.1.peg.194.
PATRIC	20591615. VBIHelPyl33062_0207.
TIGR	HP_0197.
Phylogenomic databases
HOGENOM	HBG443662.
OMA	IYYAHRL.
ProtClustDB	PRK05250.
Family and domain databases
HAMAP	MF_00086. S-AdoMet_synth1. [Tree]
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...

Entry information

Entry name

METK_HELPY

Accession

Primary (citable) accession number: P56460

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program