EzCatDB: D00087
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DB codeD00087
RLCP classification3.1144.1800.89 : Transfer
CATH domainDomain 13.40.50.170 : Rossmann foldCatalytic domain
Domain 23.10.25.10 : Methionyl-tRNA Fmet Formyltransferase; Chain A, domain 2
E.C.2.1.2.9

CATH domainRelated DB codes (homologues)
3.40.50.170 : Rossmann foldS00294

Enzyme Name
UniProtKBKEGG

P23882
Protein nameMethionyl-tRNA formyltransferasemethionyl-tRNA formyltransferase
N10-formyltetrahydrofolic-methionyl-transfer ribonucleictransformylase
formylmethionyl-transfer ribonucleic synthetase
methionyl ribonucleic formyltransferase
methionyl-tRNA Met formyltransferase
methionyl-tRNA transformylase
methionyl-transfer RNA transformylase
methionyl-transfer ribonucleate methyltransferase
methionyl-transfer ribonucleic transformylase
SynonymsEC 2.1.2.9
RefSeqNP_417746.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492145.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF02911 (Formyl_trans_C)
PF00551 (Formyl_trans_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00271Methionine metabolism
MAP00670One carbon pool by folate
MAP00970Aminoacyl-tRNA biosynthesis

UniProtKB:Accession NumberP23882
Entry nameFMT_ECOLI
Activity10-formyltetrahydrofolate + L-methionyl- tRNA(fMet) + H(2)O = tetrahydrofolate + N-formylmethionyl- tRNA(fMet).
SubunitMonomer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00001C00234C02430C00101C03294
CompoundH2O10-FormyltetrahydrofolateL-Methionyl-tRNATetrahydrofolateN-Formylmethionyl-tRNA
TypeH2Oamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamino acids,nucleic acids,sulfide groupamino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl groupamino acids,nucleic acids,sulfide group
ChEBI15377
15637

15635
20506

PubChem962
22247451
6326742
122347

91443
5460413

             
1fmtA01 UnboundUnboundUnboundUnbound
1fmtB01 UnboundUnboundUnboundUnbound
2fmtA01 UnboundUnboundUnboundBound:FME(chain C)
2fmtB01 UnboundUnboundUnboundBound:FME(chain D)
1fmtA02 UnboundUnboundUnboundUnbound
1fmtB02 UnboundUnboundUnboundUnbound
2fmtA02 UnboundUnboundUnboundUnbound
2fmtB02 UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [7]
pdbCatalytic residues
         
1fmtA01ASN 108;HIS 110;ASP 146
1fmtB01ASN 108;HIS 110;ASP 146
2fmtA01ASN 108;HIS 110;ASP 146
2fmtB01ASN 108;HIS 110;ASP 146
1fmtA02 
1fmtB02 
2fmtA02 
2fmtB02 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]

[7]p.68

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID97042366
PubMed ID8887566
JournalEMBO J
Year1996
Volume15
Pages4749-58
AuthorsSchmitt E, Blanquet S, Mechulam Y
TitleStructure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.
Related PDB1fmt
Related UniProtKBP23882
[2]
PubMed ID8727328
JournalProteins
Year1996
Volume25
Pages139-41
AuthorsSchmitt E, Mechulam Y, Ruff M, Mitschler A, Moras D, Blanquet S
TitleCrystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase.
[3]
PubMed ID9843398
JournalBiochemistry
Year1998
Volume37
Pages15925-32
AuthorsRamesh V, Gite S, RajBhandary UL
TitleFunctional interaction of an arginine conserved in the sixteen amino acid insertion module of Escherichia coli methionyl-tRNA formyltransferase with determinants for formylation in the initiator tRNA.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID99059719
PubMed ID9843487
JournalEMBO J
Year1998
Volume17
Pages6819-26
AuthorsSchmitt E, Panvert M, Blanquet S, Mechulam Y
TitleCrystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
Related PDB2fmt
Related UniProtKBP23882
[5]
PubMed ID9614118
JournalJ Biol Chem
Year1998
Volume273
Pages15085-90
AuthorsTakeuchi N, Kawakami M, Omori A, Ueda T, Spremulli LL, Watanabe K
TitleMammalian mitochondrial methionyl-tRNA transformylase from bovine liver. Purification, characterization, and gene structure.
[6]
PubMed ID10089442
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages332-4
AuthorsSchmitt E, Blanquet S, Mechulam Y
TitleCrystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f).
[7]
PubMed ID10085228
JournalBiochem J
Year1999
Volume339
Pages63-9
AuthorsNewton DT, Mangroo D
TitleMapping the active site of the Haemophilus influenzae methionyl-tRNA formyltransferase: residues important for catalysis and tRNA binding.
[8]
PubMed ID10499278
JournalFEMS Microbiol Lett
Year1999
Volume178
Pages289-98
AuthorsNewton DT, Niemkiewicz M, Lo RY, Mangroo D
TitleRecognition of the initiator tRNA by the Pseudomonas aeruginosa methionyl-tRNA formyltransferase: importance of the base-base mismatch at the end of the acceptor stem.
[9]
PubMed ID10694387
JournalBiochemistry
Year2000
Volume39
Pages2218-26
AuthorsGite S, Li Y, Ramesh V, RajBhandary UL
TitleEscherichia coli methionyl-tRNA formyltransferase: role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA.
[10]
PubMed ID10891086
JournalBiochemistry
Year2000
Volume39
Pages8039-46
AuthorsLi Y, Ramesh V, Mangroo D, Taneja C, RajBhandary UL
TitleSuppressor mutations in Escherichia coli methionyl-tRNA formyltransferase that compensate for the formylation defect of a mutant tRNA aminoacylated with lysine.
[11]
PubMed ID11274157
JournalJ Biol Chem
Year2001
Volume276
Pages20064-8
AuthorsTakeuchi N, Vial L, Panvert M, Schmitt E, Watanabe K, Mechulam Y, Blanquet S
TitleRecognition of tRNAs by Methionyl-tRNA transformylase from mammalian mitochondria.
[12]
PubMed ID11860363
JournalCurr Med Chem
Year2002
Volume9
Pages385-409
AuthorsVaughan MD, Sampson PB, Honek JF
TitleMethionine in and out of proteins: targets for drug design.
[13]
PubMed ID12087168
JournalNucleic Acids Res
Year2002
Volume30
Pages2844-50
AuthorsMayer C, RajBhandary UL
TitleConformational change of Escherichia coli initiator methionyl-tRNA(fMet) upon binding to methionyl-tRNA formyl transferase.
[14]
PubMed ID12190614
JournalPhys Rev Lett
Year2002
Volume89
Pages068103
AuthorsShen T, Canino LS, McCammon JA
TitleUnfolding proteins under external forces: a solvable model under the self-consistent pair contact probability approximation.

comments
According to the literature [7], the catalytic residues of this enzyme are the same as those of its homologous enznyme, phosphoribosylglycinamide formyltransferase (S00294 in EzCatDB), suggesting that it should have the same mechanism.

createdupdated
2004-11-252009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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