ECOLI:METH

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	metH
Protein Name(s)	Methionine synthase 5-methyltetrahydrofolate--homocysteine methyltransferase Methionine synthase, vitamin-B12-dependent MS
External Links
UniProt	P13009
EMBL	X16584 J04975 U00006 U00096 AP009048
PIR	B65209
RefSeq	NP_418443.1 YP_492162.1
PDB	1BMT 1K7Y 1K98 1MSK 3BUL 3IV9 3IVA
PDBsum	1BMT 1K7Y 1K98 1MSK 3BUL 3IV9 3IVA
ProteinModelPortal	P13009
SMR	P13009
IntAct	P13009
STRING	511145.b4019
SWISS-2DPAGE	P13009
PaxDb	P13009
PRIDE	P13009
EnsemblBacteria	AAC76989 BAE78021
GeneID	12934458 948522
KEGG	ecj:Y75_p3906 eco:b4019
PATRIC	32123567
EchoBASE	EB0582
EcoGene	EG10587
eggNOG	COG1410
HOGENOM	HOG000251409
InParanoid	P13009
KO	K00548
OMA	DYNSIMV
OrthoDB	EOG6091CH
PhylomeDB	P13009
BioCyc	EcoCyc:HOMOCYSMETB12-MONOMER ECOL316407:JW3979-MONOMER MetaCyc:HOMOCYSMETB12-MONOMER RETL1328306-WGS:GSTH-2949-MONOMER
UniPathway	UPA00051
EvolutionaryTrace	P13009
PRO	PR:P13009
Proteomes	UP000000318 UP000000625
Genevestigator	P13009
GO	GO:0005737 GO:0031419 GO:0008705 GO:0008898 GO:0008270 GO:0042558
Gene3D	1.10.1240.10 3.10.196.10 3.20.20.20 3.20.20.330 3.40.50.280
InterPro	IPR003759 IPR006158 IPR011005 IPR011822 IPR000489 IPR003726 IPR004223
Pfam	PF02310 PF02607 PF02965 PF00809 PF02574
PIRSF	PIRSF000381
SMART	SM01018
SUPFAM	SSF47644 SSF51717 SSF52242 SSF56507 SSF82282
TIGRFAMs	TIGR02082
PROSITE	PS50974 PS51332 PS51337 PS50970 PS50972

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0008705	methionine synthase activity	PMID:8572314^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008705	methionine synthase activity	PMID:23251906^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0031419	cobalamin binding	PMID:23251906^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008276	protein methyltransferase activity	PMID:8572314^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0031419	cobalamin binding	PMID:8572314^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0050667	homocysteine metabolic process	PMID:8572314^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0035999	tetrahydrofolate interconversion	PMID:8572314^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009086	methionine biosynthetic process	PMID:8572314^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008705	methionine synthase activity	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10587 MGI:MGI:894292 PANTHER:PTN001464934 RGD:621283 UniProtKB:Q99707	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[3]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10587 PANTHER:PTN001464934 UniProtKB:O33259 UniProtKB:Q99707	C	Seeded From UniProt	complete
enables	GO:0008705	methionine synthase activity	PMID:10978155^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9250984^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:2668277^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0031419	cobalamin binding	PMID:2271698^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008705	methionine synthase activity	PMID:9201956^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:9398304^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006479	protein methylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0008276	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011822	F	Seeded From UniProt	complete
enables	GO:0008705	methionine synthase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004223 InterPro:IPR011822 InterPro:IPR037010	F	Seeded From UniProt	complete
involved_in	GO:0009086	methionine biosynthetic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004223 InterPro:IPR011822 InterPro:IPR037010	P	Seeded From UniProt	complete
enables	GO:0031419	cobalamin binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006158 InterPro:IPR011822 InterPro:IPR033706 InterPro:IPR036724	F	Seeded From UniProt	complete
involved_in	GO:0042558	pteridine-containing compound metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000489	P	Seeded From UniProt	complete
involved_in	GO:0044237	cellular metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011005	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006158 InterPro:IPR036724	F	Seeded From UniProt	complete
enables	GO:0008705	methionine synthase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.1.1.13	F	Seeded From UniProt	complete
enables	GO:0031419	cobalamin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0846	F	Seeded From UniProt	complete
involved_in	GO:0009086	methionine biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0486	P	Seeded From UniProt	complete
involved_in	GO:0032259	methylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	P	Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	F	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
involved_in	GO:0008652	cellular amino acid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0028	P	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
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Drummond, JT et al. (1995) Characterization of nonradioactive assays for cobalamin-dependent and cobalamin-independent methionine synthase enzymes. Anal. Biochem. 228 323-9 PubMed GONUTS page
↑ ^2.0 ^2.1 Grabowski, M et al. (2012) Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity. Acta Biochim. Pol. 59 489-93 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
↑ Hall, DA et al. (2000) Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry 39 10711-9 PubMed GONUTS page
↑ Jarrett, JT et al. (1997) Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli. Meth. Enzymol. 281 196-213 PubMed GONUTS page
↑ Banerjee, RV et al. (1989) Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 264 13888-95 PubMed GONUTS page
↑ Banerjee, RV et al. (1990) Participation of cob(I) alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis. Biochemistry 29 11101-9 PubMed GONUTS page
↑ Goulding, CW et al. (1997) Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry 36 8082-91 PubMed GONUTS page
↑ Goulding, CW & Matthews, RG (1997) Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry 36 15749-57 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:8572314-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Drummond, JT et al. (1995) Characterization of nonradioactive assays for cobalamin-dependent and cobalamin-independent methionine synthase enzymes. Anal. Biochem. 228 323-9 PubMed GONUTS page

[PMID:23251906-2] 2.0 ^2.1 Grabowski, M et al. (2012) Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity. Acta Biochim. Pol. 59 489-93 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:10978155-4] Hall, DA et al. (2000) Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry 39 10711-9 PubMed GONUTS page

[PMID:9250984-5] Jarrett, JT et al. (1997) Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli. Meth. Enzymol. 281 196-213 PubMed GONUTS page

[PMID:2668277-6] Banerjee, RV et al. (1989) Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 264 13888-95 PubMed GONUTS page

[PMID:2271698-7] Banerjee, RV et al. (1990) Participation of cob(I) alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis. Biochemistry 29 11101-9 PubMed GONUTS page

[PMID:9201956-8] Goulding, CW et al. (1997) Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry 36 8082-91 PubMed GONUTS page

[PMID:9398304-9] Goulding, CW & Matthews, RG (1997) Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry 36 15749-57 PubMed GONUTS page

[PMID:18304323-10] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

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ECOLI:METH

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