Q8K9E5 (METK_BUCAP) 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:	BUsg_393

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	379 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-Rule MF_00086
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP-Rule MF_00086
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. HAMAP-Rule MF_00086
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
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
Gene Ontology (GO)
Biological_process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway one-carbon metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP methionine adenosyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 379	379	S-adenosylmethionine synthase HAMAP-Rule MF_00086		PRO_0000174503
Regions
	Nucleotide binding	260 – 267	8	ATP Potential
Sites
	Metal binding	17	1	Magnesium By similarity
	Metal binding	43	1	Potassium By similarity
	Metal binding	264	1	Potassium By similarity
	Metal binding	272	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9E5 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 8D5576799F7DAFE7	FASTA	379	42,003
	10 20 30 40 50 60 MTEYLFTSES VSEGHPDKIA DQISDALLDE IIKQDLKARV ACETYVKTGM VLIGGEITTT 70 80 90 100 110 120 AWVDVEEITR NTINNIGYIN SETGFDANSC AVLSTIGKQS PDITQGVDRC NPLEQGAGDQ 130 140 150 160 170 180 GIIFGYATNE TEVLMPAPIT YAHLLVKKQS ELRKKNILHW LRPDAKSQVT FKYKNGRIIG 190 200 210 220 230 240 IDTVVFSTQH KESITQDVLK EAVMEEIIKP VLPNKWLTKN TKFFINPTGR FVIGGPMGDC 250 260 270 280 290 300 GLTGRKIIVD TYGGMSRHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQLS 310 320 330 340 350 360 YAIGIAEPTS IMIETFRTGK ISNKSLINLV RNIFDLRPYG LIEMLDLLRP IYLNTAVYGH 370 FGREEFPWEK LDKVDELLQ

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67945.1.
RefSeq	NP_660734.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9E5.
SMR	Q8K9E5. Positions 3-377.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg393.
Proteomic databases
PRIDE	Q8K9E5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67945; AAM67945; BUsg_393.
GeneID	1005765.
KEGG	bas:BUsg393.
PATRIC	21247606. VBIBucAph100086_0406.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0192.
KO	K00789.
OMA	IYYAHRL.
ProtClustDB	PRK05250.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-447-MONOMER.
UniPathway	UPA00315; UER00080.
Family and domain databases
HAMAP	MF_00086. S-AdoMet_synth1.
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]
PANTHER	PTHR11964. PTHR11964. 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_BUCAP

Accession

Primary (citable) accession number: Q8K9E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program