DB code: D00083

CATH domain 1.10.155.10 : Chemotaxis Receptor Methyltransferase Cher; domain 1
3.40.50.150 : Rossmann fold Catalytic domain
E.C. 2.1.1.80
CSA 1af7
M-CSA 1af7
MACiE

CATH domain Related DB codes (homologues)
3.40.50.150 : Rossmann fold S00637 S00639 S00262 S00261 S00291 S00412 D00075 D00076 D00079 D00080 D00082 D00823

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P07801 Chemotaxis protein methyltransferase
EC 2.1.1.80
NP_460875.1 (Protein)
NC_003197.1 (DNA/RNA sequence)
PF01739 (CheR)
PF03705 (CheR_N)
[Graphical View]

KEGG enzyme name
protein-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P07801 CHER_SALTY S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00019 C00614 C00021 C04142
E.C.
Compound S-Adenosyl-L-methionine Protein glutamate S-Adenosyl-L-homocysteine Protein glutamate methyl ester
Type amino acids,amine group,nucleoside,sulfonium ion carboxyl group,peptide/protein amino acids,amine group,nucleoside,sulfide group peptide/protein
ChEBI 67040
67040
16680
57856
16680
57856
PubChem 34755
34755
25246222
439155
25246222
439155
1af7A01 Unbound Unbound Unbound Unbound
1bc5A01 Unbound Analogue:ACE-ASN-TRP-GLU-THR-PHE (chain T) Unbound Unbound
1af7A02 Unbound Unbound Bound:SAH Unbound
1bc5A02 Unbound Unbound Bound:SAH Unbound

Reference for Active-site residues
resource references E.C.
PDB;1bc5

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1af7A01
1bc5A01
1af7A02 HIS 114;HIS 192(Cobalt binding)
1bc5A02 HIS 114;HIS 192

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.554-556

References
[1]
Resource
Comments
Medline ID
PubMed ID 7567955
Journal Proteins
Year 1995
Volume 21
Pages 345-50
Authors West AH, Djordjevic S, Martinez-Hackert E, Stock AM
Title Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-284
Medline ID 97277239
PubMed ID 9115443
Journal Structure
Year 1997
Volume 5
Pages 545-58
Authors Djordjevic S, Stock AM
Title Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine.
Related PDB 1af7
Related UniProtKB P07801
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-284
Medline ID 98290446
PubMed ID 9628482
Journal Nat Struct Biol
Year 1998
Volume 5
Pages 446-50
Authors Djordjevic S, Stock AM
Title Chemotaxis receptor recognition by protein methyltransferase CheR.
Related PDB 1bc5
Related UniProtKB P07801
[4]
Resource
Comments
Medline ID
PubMed ID 9731767
Journal Nat Struct Biol
Year 1998
Volume 5
Pages 763-4
Authors Yang F, Gustafson KR, Boyd MR, Wlodawer A
Title Crystal structure of Escherichia coli HdeA.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9465023
Journal Proc Natl Acad Sci U S A
Year 1998
Volume 95
Pages 1381-6
Authors Djordjevic S, Goudreau PN, Xu Q, Stock AM, West AH
Title Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10760170
Journal Mol Microbiol
Year 2000
Volume 36
Pages 132-40
Authors Shiomi D, Okumura H, Homma M, Kawagishi I
Title The aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11916840
Journal Biophys J
Year 2002
Volume 82
Pages 1809-17
Authors Levin MD, Shimizu TS, Bray D
Title Binding and diffusion of CheR molecules within a cluster of membrane receptors.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-24 2009-02-26