EzCatDB: D00083
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DB codeD00083
CATH domainDomain 11.10.155.10 : Chemotaxis Receptor Methyltransferase Cher; domain 1
Domain 23.40.50.150 : Rossmann foldCatalytic domain
E.C.2.1.1.80
CSA1af7

CATH domainRelated DB codes (homologues)
3.40.50.150 : Rossmann foldS00637,S00639,S00262,S00261,S00291,S00412,D00075,D00076,D00079,D00080,D00082,D00823

Enzyme Name
UniProtKBKEGG

P07801
Protein nameChemotaxis protein methyltransferaseprotein-glutamate O-methyltransferase
methyl-accepting chemotaxis protein O-methyltransferase
S-adenosylmethionine-glutamyl methyltransferase
methyl-accepting chemotaxis protein methyltransferase II
S-adenosylmethionine:protein-carboxyl O-methyltransferase
protein methylase II
MCP methyltransferase I
MCP methyltransferase II
protein O-methyltransferase
protein(aspartate)methyltransferase
protein(carboxyl)methyltransferase
protein carboxyl-methylase
protein carboxyl-O-methyltransferase
protein carboxylmethyltransferase II
protein carboxymethylase
protein carboxymethyltransferase
protein methyltransferase II
SynonymsEC 2.1.1.80
RefSeqNP_460875.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PfamPF01739 (CheR)
PF03705 (CheR_N)
[Graphical view]


UniProtKB:Accession NumberP07801
Entry nameCHER_SALTY
ActivityS-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00019C00614C00021C04142
CompoundS-Adenosyl-L-methionineProtein glutamateS-Adenosyl-L-homocysteineProtein glutamate methyl ester
Typeamino acids,amine group,nucleoside,sulfonium ioncarboxyl group,peptide/proteinamino acids,amine group,nucleoside,sulfide grouppeptide/protein
ChEBI67040

16680
57856

PubChem34755

439155
25246222

            
1af7A01UnboundUnboundUnboundUnbound
1bc5A01UnboundAnalogue:ACE-ASN-TRP-GLU-THR-PHE(chain T)UnboundUnbound
1af7A02UnboundUnboundBound:SAHUnbound
1bc5A02UnboundUnboundBound:SAHUnbound

Active-site residues
resource
PDB;1bc5
pdbCofactor-binding residues
         
1af7A01 
1bc5A01 
1af7A02HIS 114;HIS 192(Cobalt binding)
1bc5A02HIS 114;HIS 192                

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.554-556

references
[1]
PubMed ID7567955
JournalProteins
Year1995
Volume21
Pages345-50
AuthorsWest AH, Djordjevic S, Martinez-Hackert E, Stock AM
TitlePurification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-284
Medline ID97277239
PubMed ID9115443
JournalStructure
Year1997
Volume5
Pages545-58
AuthorsDjordjevic S, Stock AM
TitleCrystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine.
Related PDB1af7
Related UniProtKBP07801
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-284
Medline ID98290446
PubMed ID9628482
JournalNat Struct Biol
Year1998
Volume5
Pages446-50
AuthorsDjordjevic S, Stock AM
TitleChemotaxis receptor recognition by protein methyltransferase CheR.
Related PDB1bc5
Related UniProtKBP07801
[4]
PubMed ID9731767
JournalNat Struct Biol
Year1998
Volume5
Pages763-4
AuthorsYang F, Gustafson KR, Boyd MR, Wlodawer A
TitleCrystal structure of Escherichia coli HdeA.
[5]
PubMed ID9465023
JournalProc Natl Acad Sci U S A
Year1998
Volume95
Pages1381-6
AuthorsDjordjevic S, Goudreau PN, Xu Q, Stock AM, West AH
TitleStructural basis for methylesterase CheB regulation by a phosphorylation-activated domain.
[6]
PubMed ID10760170
JournalMol Microbiol
Year2000
Volume36
Pages132-40
AuthorsShiomi D, Okumura H, Homma M, Kawagishi I
TitleThe aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction.
[7]
PubMed ID11916840
JournalBiophys J
Year2002
Volume82
Pages1809-17
AuthorsLevin MD, Shimizu TS, Bray D
TitleBinding and diffusion of CheR molecules within a cluster of membrane receptors.


createdupdated
2004-03-242009-02-26


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