EzCatDB: D00093
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DB codeD00093
CATH domainDomain 13.30.70.520 : Alpha-Beta Plaits
Domain 23.30.70.550 : Alpha-Beta Plaits
E.C.2.3.1.101


Enzyme Name
UniProtKBKEGG

Q49610
Protein nameFormylmethanofuran--tetrahydromethanopterin formyltransferaseformylmethanofuran---tetrahydromethanopterin N-formyltransferase
formylmethanofuran-tetrahydromethanopterin formyltransferase
formylmethanofuran:tetrahydromethanopterin formyltransferase
N-formylmethanofuran(CHO-MFR):tetrahydromethanopterin(H4MPT)formyltransferase
FTR
formylmethanofuran:5,6,7,8-tetrahydromethanopterinN5-formyltransferase
SynonymsEC 2.3.1.101
H4MPT formyltransferase
RefSeqNP_613403.1 (Protein)
NC_003551.1 (DNA/RNA sequence)
PfamPF01913 (FTR)
PF02741 (FTR_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00680Methane metabolism
MAP00790Folate biosynthesis

UniProtKB:Accession NumberQ49610
Entry nameFTR_METKA
ActivityFormylmethanofuran + 5,6,7,8- tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8- tetrahydromethanopterin.
SubunitHomotetramer composed of two dimers. Dimerization is sufficient for enzyme activity, but tetramerization is required for high thermostability.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01001C01217C00862C01274
CompoundFormylmethanofuran5,6,7,8-TetrahydromethanopterinMethanofuranN5-Formyl-5,6,7,8-tetrahydromethanopterin
Typeamide group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms),peptide/proteinamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,carboxyl group,phosphate group/phosphate ionamine group,aromatic ring (only carbon atom),carbohydrate,carboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms),peptide/proteinamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,carboxyl group,phosphate group/phosphate ion
ChEBI
17321


PubChem21122662
5462234
21122601
5462235
            
1ftrA01UnboundUnboundUnboundUnbound
1ftrB01UnboundUnboundUnboundUnbound
1ftrC01UnboundUnboundUnboundUnbound
1ftrD01UnboundUnboundUnboundUnbound
1ftrA02UnboundUnboundUnboundUnbound
1ftrB02UnboundUnboundUnboundUnbound
1ftrC02UnboundUnboundUnboundUnbound
1ftrD02UnboundUnboundUnboundUnbound

Active-site residues
pdb
        
1ftrA01
1ftrB01
1ftrC01
1ftrD01
1ftrA02
1ftrB02
1ftrC02
1ftrD02


references
[1]
PubMed ID8880936
JournalProteins
Year1996
Volume26
Pages118-20
AuthorsShima S, Thauer RK, Michel H, Ermler U
TitleCrystallization and preliminary X-ray diffraction studies of formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID97341227
PubMed ID9195883
JournalStructure
Year1997
Volume5
Pages635-46
AuthorsErmler U, Merckel M, Thauer R, Shima S
TitleFormylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.
Related PDB1ftr
Related UniProtKBQ49610
[3]
PubMed ID11532013
JournalEur J Biochem
Year2001
Volume268
Pages4769-75
AuthorsPomper BK, Vorholt JA
TitleCharacterization of the formyltransferase from Methylobacterium extorquens AM1.


createdupdated
2004-03-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
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)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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