Sequence of FTR_METKA
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
Q49610
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
296
31662
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 TFAEAFEAKM ARVLITAASH KWAMIAVKEA TGFGTSVIMC PAEAGIDCGY
60 VPPEETPDGR PGVTIMIGHN DEDELKEQLL DRIGQCVMTA PTASAFDAMP EAEKEDEDRV
120 GYKLSFFGDG YQEEDELDGR KVWKIPVVEG EFIVEDSFGI TTGVAGGNFY IMAESQPAGL
180 QAAEAAVDAI KGVEGAYAPF PGGIVASASK VGSKQYDFLP ASTNDAYCPT VEDNELPEGV
240 KCVYEIVING LNEEAVKEAM RVGIEAACQQ PGVVKISAGN FGGKLGQYEI HLHDLF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
419439
Shima S.,Weiss D.S.,Thauer R.K.
Formylmethanofuran:tetrahydromethanopterin formyltransferase (Ftr) from the hyperthermophilic Methanopyrus kandleri. Cloning, sequencing and functional expression of the ftr gene and one-step purification of the enzyme overproduced in Escherichia coli.
Eur. J. Biochem.
230
906-913
1995
419440
Slesarev A.I.,Mezhevaya K.V.,Makarova K.S.,Polushin N.N.,Shcherbinina O.V.,Shakhova V.V.,Belova G.I.,Aravind L.,Natale D.A.,Rogozin I.B.,Tatusov R.L.,Wolf Y.I.,Stetter K.O.,Malykh A.G.,Koonin E.V.,Kozyavkin S.A.
The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.
Proc. Natl. Acad. Sci. U.S.A.
99
4644-4649
2002
419441
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
419442
Shima S.,Thauer R.K.,Ermler U.,Durchschlag H.,Tziatzios C.,Schubert D.
A mutation affecting the association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kandleri and its influence on the enzyme's activity and thermostability.
Eur. J. Biochem.
267
6619-6623
2000
419443
Ermler U.,Merckel M.,Thauer R.,Shima S.
Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri -- new insights into salt-dependence and thermostability.
Structure
5
635-646
1997
