DB code: D00093

CATH domain	Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	RefSeq	Pfam
Q49610	Formylmethanofuran--tetrahydromethanopterin formyltransferase	EC 2.3.1.101 H4MPT formyltransferase	NP_613403.1 (Protein) NC_003551.1 (DNA/RNA sequence)	PF01913 (FTR) PF02741 (FTR_C) [Graphical View]

KEGG enzyme name
formylmethanofuran---tetrahydromethanopterin N-formyltransferase formylmethanofuran-tetrahydromethanopterin formyltransferase formylmethanofuran:tetrahydromethanopterin formyltransferase N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT)formyltransferase FTR formylmethanofuran:5,6,7,8-tetrahydromethanopterinN5-formyltransferase

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
Q49610	FTR_METKA	Formylmethanofuran + 5,6,7,8- tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8- tetrahydromethanopterin.	Homotetramer composed of two dimers. Dimerization is sufficient for enzyme activity, but tetramerization is required for high thermostability.	Cytoplasm.

Compound table
	Substrates		Products		Intermediates
KEGG-id	C01001	C01217	C00862	C01274
E.C.
Compound	Formylmethanofuran	5,6,7,8-Tetrahydromethanopterin	Methanofuran	N5-Formyl-5,6,7,8-tetrahydromethanopterin
Type	amide group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms),peptide/protein	amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,carboxyl group,phosphate group/phosphate ion	amine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms),peptide/protein	amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,carboxyl group,phosphate group/phosphate ion
ChEBI		17321 17321
PubChem	21122662 21122662	5462234 5462234	21122601 21122601	5462235 5462235

1ftrA01	Unbound	Unbound	Unbound	Unbound
1ftrB01	Unbound	Unbound	Unbound	Unbound
1ftrC01	Unbound	Unbound	Unbound	Unbound
1ftrD01	Unbound	Unbound	Unbound	Unbound
1ftrA02	Unbound	Unbound	Unbound	Unbound
1ftrB02	Unbound	Unbound	Unbound	Unbound
1ftrC02	Unbound	Unbound	Unbound	Unbound
1ftrD02	Unbound	Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1ftrA01
1ftrB01
1ftrC01
1ftrD01
1ftrA02
1ftrB02
1ftrC02
1ftrD02

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID	8880936
Journal	Proteins
Year	1996
Volume	26
Pages	118-20
Authors	Shima S, Thauer RK, Michel H, Ermler U
Title	Crystallization and preliminary X-ray diffraction studies of formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri.
Related PDB
Related UniProtKB
[2]
Resource
Comments	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID	97341227
PubMed ID	9195883
Journal	Structure
Year	1997
Volume	5
Pages	635-46
Authors	Ermler U, Merckel M, Thauer R, Shima S
Title	Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.
Related PDB	1ftr
Related UniProtKB	Q49610
[3]
Resource
Comments
Medline ID
PubMed ID	11532013
Journal	Eur J Biochem
Year	2001
Volume	268
Pages	4769-75
Authors	Pomper BK, Vorholt JA
Title	Characterization of the formyltransferase from Methylobacterium extorquens AM1.
Related PDB
Related UniProtKB

Comments

Created	Updated
2004-03-17	2009-02-26