Sequence of FTR_METBF
EC Number:2.3.1.101
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
formylmethanofuran-tetrahydromethanopterin N-formyltransferase
P55301
Methanosarcina barkeri (strain Fusaro / DSM 804)
297
31697
Reaction
formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8-tetrahydromethanopterin
Other sequences found for EC No. 2.3.1.101
General information:
Sequence
0 MEINGVEIED TYAEAFPIKI ARVLITAATK RWALVAATEA TGFATSVIMC PAEAGIERLA
60 SPSETPDGRP GVYVQICTFK YEALEEQLLE RIGQCVLTAP TTAVFNGLPE AEKQFNVGFK
120 LKFFADGMES ETQIAGRKVY KVPIMEGDFL AEENIGAIAG IAGGNFFIFG DSQMTALTAA
180 EAAVDTIAEL EGTITPFPGG IVASGSKSGA NKYKFLKATA NERFCPSIKD KIENTEIPAD
240 VNAVYEIVIN GLDEESIKAA MKAGIKAAVT VPGVKKISAG NYGGKLGKYQ FKLHELF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
800334
Kunow J.,Shima S.,Vorholt J.A.,Thauer R.K.
Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: comparison with the enzymes from thermophilic and hyperthermophilic methanogens.
Arch. Microbiol.
165
97-105
1996
800335
Maeder D.L.,Anderson I.,Brettin T.S.,Bruce D.C.,Gilna P.,Han C.S.,Lapidus A.,Metcalf W.W.,Saunders E.,Tapia R.,Sowers K.R.
The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes.
J. Bacteriol.
188
7922-7931
2006
800336
Breitung J.,Borner G.,Scholz S.,Linder D.,Stetter K.O.,Thauer R.K.
Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri.
Eur. J. Biochem.
210
971-981
1992
800337
Mamat B.,Roth A.,Grimm C.,Ermler U.,Tziatzios C.,Schubert D.,Thauer R.K.,Shima S.
Crystal structures and enzymatic properties of three formyltransferases from archaea: environmental adaptation and evolutionary relationship.
Protein Sci.
11
2168-2178
2002
