Gene Details


gene name: metH


locus tag k12ECK4011 Crenarchaeota Euryarchaeota Nanoarcheota Alphaproteobacteria Betaproteobacteria Gammaproteobacteria Deltaproteobacteria Epsilonproteobacteria Cyanobacteria Actinobacteridae Firmicutes Spirochaetes others Protist Microsporidia Fungi Metazoa Plantae
information on phylogenetic profile
locus tag mg1655b4019
locus tag w3110JW3979
gene name k12metH
locus namemetH
synonyms of locus name

scop id51717; 52242; 56507; 47644
superfamilyDihydropteroate synthetase-like; Cobalamin (vitamin B12)-binding domain; Methionine synthase (activation domain); Methionine synthase domain
pfam idPF02965; PF02607; PF02310; PF00809; PF02574
pfam domainVitamin B12-dep methionine synthase; B12 binding; B12 binding domain; Pterin binding enzyme; Homocysteine S-methyltransferase
tigrfam idTIGR02082
namemetH
function5-methyltetrahydrofolate--homocysteine

swissprot nameMETH_ECOLI
descriptionMethionine synthase (EC 2.1.1.13) (5-methyltetrahydrofolate--|homocysteine methyltransferase) (Methionine synthase, vitamin-B12-|dependent) (MS).
seq length1226
fastaseq

go idGO:0009086; GO:0009257; GO:0009257; GO:0009236; GO:0006556; GO:0009257
go termmethionine biosynthesis; 10-formyltetrahydrofolate biosynthesis; 10-formylTHF biosyn; vitamin B12 biosynthesis; S-adenosylmethionine biosynthesis; 10-formylTHF biosynth

gene product descriptionhomocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent
comment gene product description
evidenceE
context
gene product descEnzyme
cell locationCytoplasmic
featuresCDS

functional category codeE
functional categoryAmino acid transport and metabolism

reference #1Domain alternation switches B(12)-dependent methionine synthase to the activation conformation.

Bandarian V., Pattridge K., Lennon B., Huddler D., Matthews R., Ludwig M. (Nat Struct Biol. 2002 Jan; 9(1):53-6)
reference #2Cloning 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.

Banerjee R., Johnston N., Sobeski J., Datta P., Matthews R. (J Biol Chem. 1989 Aug 15; 264(23):13888-95)
reference #3Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.

Blattner F., Burland V., Plunkett G., Sofia H., Daniels D. (Nucleic Acids Res. 1993 Nov 25; 21(23):5408-17)
reference #4Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli.

Luschinsky C., Drummond J., Matthews R., Ludwig M. (J Mol Biol. 1992 May 20; 225(2):557-60)
reference #5Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2.

Old I., Margarita D., Glass R., Saint Girons I. (Gene. 1990 Mar 1; 87(1):15-21)
reference #6Cobalamin-dependent methionine synthase.

Banerjee R., Matthews R. (FASEB J. 1990 Mar; 4(5):1450-9)
reference #7Cloning 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.

Banerjee R., Johnston N., Sobeski J., Datta P., Matthews R. (J Biol Chem. 1989 Aug 15; 264(23):13888-95)
reference #8How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase.

Drennan C., Huang S., Drummond J., Matthews R., Lidwig M. (Science. 1994 Dec 9; 266(5191):1669-74)
reference #9Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase.

Drummond J., Loo R., Matthews R. (Biochemistry. 1993 Sep 14; 32(36):9282-9)
reference #10The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12.

Dixon M., Huang S., Matthews R., Ludwig M. (Structure. 1996 Nov 15; 4(11):1263-75)
reference #11Two enzymic mechanisms for the methylation of homocysteine by extracts of Escherichia coli.

Foster M., Tejerina G., Guest J., Woods D. (Biochem J. 1964 Sep; 92(3):476-88)

phylogenetic profile
 
1 1 1 1 115 1 52 1 105 1 122 122 1 1 1 1 1 1 1 1
568 544 533 1 536 532 447 535 560 1 552 566 381 1 1 1455 1 1 1440 1471
1472 1074 142 1468 1 1 1 1464 1 1433 1430 1431 1 1064 1543 1 1 1507 1068 581
553 518 502 528 551 572 577 1 318 315 346 1 1 1 1 475 726 731 727 737
731 130 1252 75 308 1 1 122 1 130 128 128 128 128 1 1 1 1 1 1
1 1 60 1 109 111 110 111 110 124 124 118 1 1 1 1 1 1 1 354
1 1513 1 1 1 1 1 2096 2401 2408 2406 1 1 1 1558 1683 1 1 1622 1599
1603 2326 2332 2326 1608 2394 2395 1853 1825 1846 1 1108 1111 1 1 2097 2097 2098 1 1043
1049 1 1 1 1 1 1 1455 1343 213 1 1318 1 289 584 1 1414 1 1 1414
54 1 1 1 1 1 1 1 410 1251 1253 60 1264 1173 1 85 1 1 1