Sequence of OXC_OXAFO
EC Number:4.1.1.8
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
oxalyl-CoA = formyl-CoA + CO2
Other sequences found for EC No. 4.1.1.8
General information:
Sequence
0 MSNDDNVELT DGFHVLIDAL KMNDIDTMYG VVGIPITNLA RMWQDDGQRF YSFRHEQHAG
60 YAASIAGYIE GKPGVCLTVS APGFLNGVTS LAHATTNCFP MILLSGSSER EIVDLQQGDY
120 EEMDQMNVAR PHCKASFRIN SIKDIPIGIA RAVRTAVSGR PGGVYVDLPA KLFGQTISVE
180 EANKLLFKPI DPAPAQIPAE DAIARAADLI KNAKRPVIML GKGAAYAQCD DEIRALVEET
240 GIPFLPMGMA KGLLPDNHPQ SAAATRAFAL AQCDVCVLIG ARLNWLMQHG KGKTWGDELK
300 KYVQIDIQAN EMDSNQPIAA PVVGDIKSAV SLLRKALKGA PKADAEWTGA LKAKVDGNKA
360 KLAGKMTAET PSGMMNYSNS LGVVRDFMLA NPDISLVNEG ANALDNTRMI VDMLKPRKRL
420 DSGTWGVMGI GMGYCVAAAA VTGKPVIAVE GDSAFGFSGM ELETICRYNL PVTVIIMNNG
480 GIYKGNEADP QPGVISCTRL TRGRYDMMME AFGGKGYVAN TPAELKAALE EAVASGKPCL
540 INAMIDPDAG VESGRIKSLN VVSKVGKK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
70695
Lung H.-Y.,Baetz A.L.,Peck A.B.
Molecular cloning, DNA sequence, and gene expression of the oxalyl-coenzyme A decarboxylase gene, oxc, from the bacterium Oxalobacter formigenes.
J. Bacteriol.
176
2468-2472
1994
70696
Berthold C.L.,Moussatche P.,Richards N.G.,Lindqvist Y.
Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate.
J. Biol. Chem.
280
41645-41654
2005
70697
Berthold C.L.,Toyota C.G.,Moussatche P.,Wood M.D.,Leeper F.,Richards N.G.,Lindqvist Y.
Crystallographic snapshots of oxalyl-CoA decarboxylase give insights into catalysis by nonoxidative ThDP-dependent decarboxylases.
Structure
15
853-861
2007
