ECMDB

Identification

Name:

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase

Synonyms:

Cobalamin-independent methionine synthase
Methionine synthase, vitamin-B12 independent isozyme

Gene Name:

metE

Enzyme Class:

2.1.1.14

Biological Properties

General Function:

Involved in 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity

Specific Function:

Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation

Cellular Location:

Not Available

SMPDB Pathways:

methionine biosynthesis PW000814

KEGG Pathways:

Cysteine and methionine metabolism ec00270
Metabolic pathways eco01100
Selenoamino acid metabolism ec00450

KEGG Reactions:

1.0

↔

1.0

1.05-Methyltetrahydrofolic acid + 1.0L-Homocysteine ↔ 1.0Hydrogen ion + 1.0L-Methionine + 1.0Tetrahydrofolic acid
ReactionCard

1.0

↔

1.0

1.05-Methyltetrahydropteroyltri-L-glutamic acid + 1.0L-Homocysteine ↔ 1.0Tetrahydropteroyltri-L-glutamic acid + 1.0L-Methionine
ReactionCard

SMPDB Reactions:

1.0Homocysteine

1.0

→

1.0

1.0Homocysteine + 1.0 N5-methyl--tetrahydropteroyl tri-L-glutamate + 1.0Homocysteine → 1.0L-Methionine + 1.0tetrahydropteroyltri-L-glutamate
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.05-Methyltetrahydrofolic acid + 1.0L-Homocysteine ↔ 1.0Hydrogen ion + 1.0L-Methionine + 1.0Tetrahydrofolic acid
ReactionCard

1.0

→

1.0

1.0tetrahydropteroyl tri-L-glutamate

1.0L-Homocysteine + 1.05-Methyltetrahydropteroyltri-L-glutamic acid → 1.0L-Methionine + 1.0tetrahydropteroyl tri-L-glutamate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.05-methyltetrahydropteroyltri-L-glutamate + 1.0L-Homocysteine → 1.0tetrahydropteroyltri-L-glutamate + 1.0L-Methionine
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB24199	N5-methyl--tetrahydropteroyl tri-L-glutamate	MetaboCard
ECMDB01396	5-Methyltetrahydrofolic acid	MetaboCard
ECMDB23154	5-methyltetrahydropteroyltri-L-glutamate	MetaboCard
ECMDB01079	5-Methyltetrahydropteroyltri-L-glutamic acid	MetaboCard
ECMDB24053	Homocysteine	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00165	L-Homocysteine	MetaboCard
ECMDB00696	L-Methionine	MetaboCard
ECMDB21010	Selenohomocysteine	MetaboCard
ECMDB01846	Tetrahydrofolic acid	MetaboCard
ECMDB23160	tetrahydropteroyltri-L-glutamate	MetaboCard
ECMDB01174	Tetrahydropteroyltri-L-glutamic acid	MetaboCard

GO Classification:

Function
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
binding
catalytic activity
cation binding
ion binding
metal ion binding
methyltransferase activity
S-methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
transition metal ion binding
zinc ion binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process
methionine biosynthetic process
sulfur amino acid biosynthetic process
sulfur amino acid metabolic process

Gene Properties

Blattner:

b3829

Gene Orientation

Clockwise

Centisome Percentage:

86.45

Left Sequence End

4011076

Right Sequence End

4013337

Gene Sequence:

>2262 bp
ATGATCAAGTTATCTGAAAAAGGCGTGTTTCTCGCCAGTAATAACGAAATAATTGCCGAA
GAACATTTCACCGGCGAAATTAAAAAAGAAGAAGCCAAAAAAGGCACTATTGCCTGGTCT
ATTCTCTCTTCGCATAATACGTCCGGAAATATGGATAAACTTAAAATTAAGTTTGATTCA
TTAGCCTCTCACGATATTACCTTTGTTGGTATTGTACAGACCGCTAAAGCGTCCGGTATG
GAACGTTTCCCGCTGCCGTATGTGCTGACCAACTGCCATAACTCACTCTGCGCCGTCGGC
GGCACTATTAACGGTGATGACCATGTTTTTGGTTTATCGGCGGCCCAGCGTTATGGCGGT
ATTTTTGTGCCTCCGCATATTGCGGTCATCCATCAATATATGCGTGAGATGATGGCAGGC
GGCGGCAAAATGATCCTCGGGTCAGACAGCCACACCCGTTACGGTGCATTAGGGACAATG
GCAGTCGGTGAGGGCGGCGGTGAGTTGGTAAAACAGCTGCTTAATGACACCTGGGATATC
GACTATCCGGGCGTGGTTGCGGTGCATCTGACCGGAAAACCTGCGCCGTATGTGGGGCCA
CAGGATGTGGCGCTGGCTATCATTGGCGCGGTGTTCAAAAACGGTTACGTCAAAAACAAA
GTCATGGAGTTCGTTGGACCGGGCGTTAGCGCGCTCTCTACCGATTTCCGTAACAGCGTT
GACGTGATGACCACTGAAACGACCTGTTTAAGTTCTGTCTGGCAAACCGATGAAGAAGTC
CATAACTGGCTGGCGCTGCACGGTCGCGGCCAGGATTACTGCCAGCTTAACCCTCAACCG
ATGGCGTACTACGATGGCTGCATCAGCGTTGATTTAAGCGCCATCAAACCAATGATTGCG
CTGCCGTTCCACCCGAGCAACGTGTATGAAATCGACACACTGAACCAGAACCTGACCGAC
ATTCTGCGTGAGATTGAAATTGAGTCCGAACGCGTGGCGCACGGTAAAGCCAAACTCTCG
CTGCTGGATAAAGTGGAAAATGGTCGCCTGAAAGTGCAGCAGGGGATTATCGCGGGCTGT
TCTGGCGGTAACTACGAAAACGTCATCGCGGCGGCGAATGCACTGCGCGGTCAATCCTGT
GGCAATGACACCTTCTCGCTGGCAGTTTACCCGTCATCACAGCCGGTGTTTATGGATCTC
GCCAAAAAAGGTGTGGTAGCAGATTTGATTGGCGCAGGCGCAATCATCAGAACCGCGTTC
TGCGGCCCATGCTTTGGCGCGGGCGATACGCCAATCAACAACGGTTTGAGTATTCGCCAC
ACCACGCGTAACTTCCCGAACCGCGAAGGCTCTAAGCCAGCTAATGGGCAGATGTCAGCG
GTGGCGTTGATGGACGCTCGTTCTATCGCTGCGACTGCGGCAAACGGTGGCTATTTAACC
TCTGCCAGCGAACTTGATTGCTGGGACAACGTGCCGGAGTACGCCTTCGATGTAACGCCG
TATAAAAACCGTGTTTATCAGGGCTTTGTGAAAGGGGCAACTCAGCAACCGCTGATTTAC
GGGCCGAACATTAAAGACTGGCCGGAATTGGGTGCGCTGACTGACAATATCGTCCTGAAA
GTGTGCTCGAAGATCCTCGACGAAGTGACCACCACCGACGAACTGATTCCTTCCGGTGAA
ACCTCTTCTTATCGTTCAAATCCGATTGGTCTGGCGGAGTTTACCCTGTCTCGCCGCGAT
CCCGGTTATGTTAGCAGAAGTAAAGCGACTGCTGAGCTGGAAAATCAGCGTCTGGCGGGG
AATGTCAGCGAGCTGACAGAGGTGTTTGCGCGCATTAAGCAGATTGCTGGTCAGGAGCAT
ATTGATCCGCTGCAAACTGAAATTGGCAGCATGGTCTATGCGGTGAAACCAGGCGATGGT
TCTGCGCGTGAACAGGCGGCGAGCTGCCAGCGTGTGATTGGCGGTCTGGCGAATATTGCC
GAGGAGTACGCGACTAAACGCTATCGTTCTAACGTCATCAACTGGGGGATGTTACCGCTG
CAAATGGCGGAAGTACCAACCTTTGAAGTGGGGGATTACATTTACATCCCTGGCATTAAA
GCGGCGCTGGATAATCCGGGTACGACGTTTAAAGGTTATGTGATCCATGAAGATGCGCCG
GTAACGGAAATTACGCTCTATATGGAAAGTCTGACTGCTGAAGAGCGCGAGATTATCAAG
GCGGGTAGTTTGATTAACTTCAATAAAAACCGTCAGATGTAA

Protein Properties

Pfam Domain Function:

Meth_synt_1 (PF08267 )
Meth_synt_2 (PF01717 )

Protein Residues:

753

Protein Molecular Weight:

84673

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
MTILNHTLGFPRVGLRRELKKAQESYWAGNSTREELLAVGRELRARHWDQQKQAGIDLLP
VGDFAWYDHVLTTSLLLGNVPARHQNKDGSVDIDTLFRIGRGRAPTGEPAAAAEMTKWFN
TNYHYMVPEFVKGQQFKLTWTQLLDEVDEALALGHKVKPVLLGPVTWLWLGKVKGEQFDR
LSLLNDILPVYQQVLAELAKRGIEWVQIDEPALVLELPQAWLDAYKPAYDALQGQVKLLL
TTYFEGVTPNLDTITALPVQGLHVDLVHGKDDVAELHKRLPSDWLLSAGLINGRNVWRAD
LTEKYAQIKDIVGKRDLWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCHELALLR
DALNSGDTAALAEWSAPIQARRHSTRVHNPAVEKRLAAITAQDSQRANVYEVRAEAQRAR
FKLPAWPTTTIGSFPQTTEIRTLRLDFKKGNLDANNYRTGIAEHIKQAIVEQERLGLDVL
VHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPIVIGDISRPAPITVEWAKYA
QSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDE
PALREGLPLRRSDWDAYLQWGVEAFRINAAVAKDDTQIHTHMCYCEFNDIMDSIAALDAD
VITIETSRSDMELLESFEEFDYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAKRIPAERL
WVNPDCGLKTRGWPETRAALANMVQAAQNLRRG

References

External Links:

Resource	Link
Uniprot ID:	P25665
Uniprot Name:	METE_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674754
Ecogene ID:	EG10584
Ecocyc:	EG10584
ColiBase:	b3829
Kegg Gene:	b3829
EchoBASE ID:	EB0579
CCDB:	METE_ECOLI
BacMap:	16131678

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
Gonzalez, J. C., Banerjee, R. V., Huang, S., Sumner, J. S., Matthews, R. G. (1992). "Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem." Biochemistry 31:6045-6056. Pubmed: 1339288
Gonzalez, J. C., Peariso, K., Penner-Hahn, J. E., Matthews, R. G. (1996). "Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme." Biochemistry 35:12228-12234. Pubmed: 8823155
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
Maxon, M. E., Redfield, B., Cai, X. Y., Shoeman, R., Fujita, K., Fisher, W., Stauffer, G., Weissbach, H., Brot, N. (1989). "Regulation of methionine synthesis in Escherichia coli: effect of the MetR protein on the expression of the metE and metR genes." Proc Natl Acad Sci U S A 86:85-89. Pubmed: 2643109
Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
Zhou, Z. S., Peariso, K., Penner-Hahn, J. E., Matthews, R. G. (1999). "Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli." Biochemistry 38:15915-15926. Pubmed: 10625458

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (P25665)