ECOLI:METK

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	metK (synonyms: metX)
Protein Name(s)	S-adenosylmethionine synthase AdoMet synthase MAT Methionine adenosyltransferase
External Links
UniProt	P0A817
EMBL	K02129 U28377 U00096 AP009048 M98266 M31770
PIR	E65079
RefSeq	NP_417417.1 YP_491141.1
PDB	1FUG 1MXA 1MXB 1MXC 1P7L 1RG9 1XRA 1XRB 1XRC
PDBsum	1FUG 1MXA 1MXB 1MXC 1P7L 1RG9 1XRA 1XRB 1XRC
ProteinModelPortal	P0A817
SMR	P0A817
DIP	DIP-35672N
IntAct	P0A817
MINT	MINT-1233798
STRING	511145.b2942
PhosSite	P0809415
SWISS-2DPAGE	P0A817
PaxDb	P0A817
PRIDE	P0A817
EnsemblBacteria	AAC75979 BAE77005
GeneID	12931663 945389
KEGG	ecj:Y75_p2872 eco:b2942
PATRIC	32121294
EchoBASE	EB0584
EcoGene	EG10589
eggNOG	COG0192
HOGENOM	HOG000245710
InParanoid	P0A817
KO	K00789
OMA	IGEQSPD
OrthoDB	EOG68WR6M
PhylomeDB	P0A817
BioCyc	EcoCyc:S-ADENMETSYN-MONOMER ECOL316407:JW2909-MONOMER MetaCyc:S-ADENMETSYN-MONOMER
SABIO-RK	P0A817
UniPathway	UPA00315
EvolutionaryTrace	P0A817
PRO	PR:P0A817
Proteomes	UP000000318 UP000000625
Genevestigator	P0A817
GO	GO:0005829 GO:0005524 GO:0042802 GO:0000287 GO:0004478 GO:0030955 GO:0006730 GO:0006556 GO:0033353
HAMAP	MF_00086
InterPro	IPR022631 IPR022630 IPR022629 IPR022628 IPR002133 IPR022636
PANTHER	PTHR11964
Pfam	PF02773 PF02772 PF00438
PIRSF	PIRSF000497
SUPFAM	SSF55973
TIGRFAMs	TIGR01034
PROSITE	PS00376 PS00377

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0033353	S-adenosylmethionine cycle	PMID:11952912^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10589 PANTHER:PTN000239344 RGD:3050 RGD:619985 TAIR:locus:2058011 TAIR:locus:2141385 TAIR:locus:2196160 UniProtKB:P9WGV1	C	Seeded From UniProt	complete
enables	GO:0004478	methionine adenosyltransferase activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10589 MGI:MGI:2443731 PANTHER:PTN000239344 PomBase:SPBC14F5.05c RGD:3050 RGD:619985 SGD:S000002910 SGD:S000004170 TAIR:locus:2058011 TAIR:locus:2196160 UniProtKB:P31153 UniProtKB:Q00266	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:8611562^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A817	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0A817	F	Seeded From UniProt	complete
enables	GO:0030955	potassium ion binding	PMID:7629147^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0030955	potassium ion binding	PMID:6251075^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006556	S-adenosylmethionine biosynthetic process	PMID:4577753^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006556	S-adenosylmethionine biosynthetic process	PMID:2115868^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:17309111^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:17272300^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004478	methionine adenosyltransferase activity	PMID:6251075^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:6251075^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004478	methionine adenosyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002133 InterPro:IPR022628 InterPro:IPR022629 InterPro:IPR022630 InterPro:IPR022631 InterPro:IPR022636	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002133	F	Seeded From UniProt	complete
involved_in	GO:0006556	S-adenosylmethionine biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002133 InterPro:IPR022628 InterPro:IPR022629 InterPro:IPR022630 InterPro:IPR022631 InterPro:IPR022636	P	Seeded From UniProt	complete
enables	GO:0004478	methionine adenosyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.5.1.6	F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076340	F	Seeded From UniProt	complete
involved_in	GO:0006730	one-carbon metabolic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076340	P	Seeded From UniProt	complete
enables	GO:0004478	methionine adenosyltransferase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076340	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076340	C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076340	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0006730	one-carbon metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0554	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
involved_in	GO:0006556	S-adenosylmethionine biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00315	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Wei, Y & Newman, EB (2002) Studies on the role of the metK gene product of Escherichia coli K-12. Mol. Microbiol. 43 1651-6 PubMed GONUTS page
↑ ^2.0 ^2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ ^3.0 ^3.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Takusagawa, F et al. (1996) Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution. Biochemistry 35 2586-96 PubMed GONUTS page
↑ McQueney, MS & Markham, GD (1995) Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition. J. Biol. Chem. 270 18277-84 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Markham, GD et al. (1980) S-Adenosylmethionine synthetase from Escherichia coli. J. Biol. Chem. 255 9082-92 PubMed GONUTS page
↑ Greene, RC et al. (1973) Properties of metK mutants of Escherichia coli K-12. J. Bacteriol. 115 57-67 PubMed GONUTS page
↑ Satishchandran, C et al. (1990) Novel Escherichia coli K-12 mutants impaired in S-adenosylmethionine synthesis. J. Bacteriol. 172 4489-96 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
↑ Watt, RM et al. (2007) Visualizing the proteome of Escherichia coli: an efficient and versatile method for labeling chromosomal coding DNA sequences (CDSs) with fluorescent protein genes. Nucleic Acids Res. 35 e37 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:11952912-1] Wei, Y & Newman, EB (2002) Studies on the role of the metK gene product of Escherichia coli K-12. Mol. Microbiol. 43 1651-6 PubMed GONUTS page

[PMID:16858726-2] 2.0 ^2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:21873635-3] 3.0 ^3.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8611562-4] Takusagawa, F et al. (1996) Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution. Biochemistry 35 2586-96 PubMed GONUTS page

[PMID:7629147-5] McQueney, MS & Markham, GD (1995) Investigation of monovalent cation activation of S-adenosylmethionine synthetase using mutagenesis and uranyl inhibition. J. Biol. Chem. 270 18277-84 PubMed GONUTS page

[PMID:6251075-6] 6.0 ^6.1 ^6.2 Markham, GD et al. (1980) S-Adenosylmethionine synthetase from Escherichia coli. J. Biol. Chem. 255 9082-92 PubMed GONUTS page

[PMID:4577753-7] Greene, RC et al. (1973) Properties of metK mutants of Escherichia coli K-12. J. Bacteriol. 115 57-67 PubMed GONUTS page

[PMID:2115868-8] Satishchandran, C et al. (1990) Novel Escherichia coli K-12 mutants impaired in S-adenosylmethionine synthesis. J. Bacteriol. 172 4489-96 PubMed GONUTS page

[PMID:18304323-9] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:17309111-10] Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page

[PMID:17272300-11] Watt, RM et al. (2007) Visualizing the proteome of Escherichia coli: an efficient and versatile method for labeling chromosomal coding DNA sequences (CDSs) with fluorescent protein genes. Nucleic Acids Res. 35 e37 PubMed GONUTS page

[PMID:15911532-12] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:METK

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