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ECOLI:METH

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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 Extension 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

Notes

References

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

  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
  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
  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
  4. Hall, DA et al. (2000) Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry 39 10711-9 PubMed GONUTS page
  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
  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
  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
  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
  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
  10. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page