DB code: D00087

RLCP classification 3.1144.1800.89 : Transfer
CATH domain 3.40.50.170 : Rossmann fold Catalytic domain
3.10.25.10 : Methionyl-tRNA Fmet Formyltransferase; Chain A, domain 2
E.C. 2.1.2.9
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.170 : Rossmann fold S00294

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P23882 Methionyl-tRNA formyltransferase
EC 2.1.2.9
NP_417746.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492145.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF02911 (Formyl_trans_C)
PF00551 (Formyl_trans_N)
[Graphical View]

KEGG enzyme name
methionyl-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P23882 FMT_ECOLI 10-formyltetrahydrofolate + L-methionyl- tRNA(fMet) + H(2)O = tetrahydrofolate + N-formylmethionyl- tRNA(fMet). Monomer.

KEGG Pathways
Map code Pathways E.C.
MAP00271 Methionine metabolism
MAP00670 One carbon pool by folate
MAP00970 Aminoacyl-tRNA biosynthesis

Compound table
Substrates Products Intermediates
KEGG-id C00001 C00234 C02430 C00101 C03294
E.C.
Compound H2O 10-Formyltetrahydrofolate L-Methionyl-tRNA Tetrahydrofolate N-Formylmethionyl-tRNA
Type H2O amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group amino acids,nucleic acids,sulfide group amino acids,amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carboxyl group amino acids,nucleic acids,sulfide group
ChEBI 15377
15637
15635
20506
PubChem 22247451
962
122347
6326742
5460413
91443
1fmtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1fmtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2fmtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FME (chain C)
2fmtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:FME (chain D)
1fmtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1fmtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2fmtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2fmtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fmtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 108;HIS 110;ASP 146
1fmtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 108;HIS 110;ASP 146
2fmtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 108;HIS 110;ASP 146
2fmtB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 108;HIS 110;ASP 146
1fmtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fmtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2fmtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2fmtB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
[7]
p.68

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 97042366
PubMed ID 8887566
Journal EMBO J
Year 1996
Volume 15
Pages 4749-58
Authors Schmitt E, Blanquet S, Mechulam Y
Title Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.
Related PDB 1fmt
Related UniProtKB P23882
[2]
Resource
Comments
Medline ID
PubMed ID 8727328
Journal Proteins
Year 1996
Volume 25
Pages 139-41
Authors Schmitt E, Mechulam Y, Ruff M, Mitschler A, Moras D, Blanquet S
Title Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9843398
Journal Biochemistry
Year 1998
Volume 37
Pages 15925-32
Authors Ramesh V, Gite S, RajBhandary UL
Title Functional 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS)
Medline ID 99059719
PubMed ID 9843487
Journal EMBO J
Year 1998
Volume 17
Pages 6819-26
Authors Schmitt E, Panvert M, Blanquet S, Mechulam Y
Title Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.
Related PDB 2fmt
Related UniProtKB P23882
[5]
Resource
Comments
Medline ID
PubMed ID 9614118
Journal J Biol Chem
Year 1998
Volume 273
Pages 15085-90
Authors Takeuchi N, Kawakami M, Omori A, Ueda T, Spremulli LL, Watanabe K
Title Mammalian mitochondrial methionyl-tRNA transformylase from bovine liver. Purification, characterization, and gene structure.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10089442
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 332-4
Authors Schmitt E, Blanquet S, Mechulam Y
Title Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f).
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10085228
Journal Biochem J
Year 1999
Volume 339
Pages 63-9
Authors Newton DT, Mangroo D
Title Mapping the active site of the Haemophilus influenzae methionyl-tRNA formyltransferase: residues important for catalysis and tRNA binding.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10499278
Journal FEMS Microbiol Lett
Year 1999
Volume 178
Pages 289-98
Authors Newton DT, Niemkiewicz M, Lo RY, Mangroo D
Title Recognition of the initiator tRNA by the Pseudomonas aeruginosa methionyl-tRNA formyltransferase: importance of the base-base mismatch at the end of the acceptor stem.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10694387
Journal Biochemistry
Year 2000
Volume 39
Pages 2218-26
Authors Gite S, Li Y, Ramesh V, RajBhandary UL
Title Escherichia 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.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10891086
Journal Biochemistry
Year 2000
Volume 39
Pages 8039-46
Authors Li Y, Ramesh V, Mangroo D, Taneja C, RajBhandary UL
Title Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase that compensate for the formylation defect of a mutant tRNA aminoacylated with lysine.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11274157
Journal J Biol Chem
Year 2001
Volume 276
Pages 20064-8
Authors Takeuchi N, Vial L, Panvert M, Schmitt E, Watanabe K, Mechulam Y, Blanquet S
Title Recognition of tRNAs by Methionyl-tRNA transformylase from mammalian mitochondria.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11860363
Journal Curr Med Chem
Year 2002
Volume 9
Pages 385-409
Authors Vaughan MD, Sampson PB, Honek JF
Title Methionine in and out of proteins: targets for drug design.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 12087168
Journal Nucleic Acids Res
Year 2002
Volume 30
Pages 2844-50
Authors Mayer C, RajBhandary UL
Title Conformational change of Escherichia coli initiator methionyl-tRNA(fMet) upon binding to methionyl-tRNA formyl transferase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12190614
Journal Phys Rev Lett
Year 2002
Volume 89
Pages 068103
Authors Shen T, Canino LS, McCammon JA
Title Unfolding proteins under external forces: a solvable model under the self-consistent pair contact probability approximation.
Related PDB
Related UniProtKB

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.

Created Updated
2004-11-25 2009-02-26