|Domain Trusted Cutoff||243.40|
|Domain Noise Cutoff||146.85|
|Entry Date||Oct 30 2006 1:13PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis,
at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase.|
RM PMID: 15978081
RT HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis.
RA Yurimoto H, Hirai R, Matsuno N, Yasueda H, Kato N, Sakai Y
RL Mol Microbiol. 2005 Jul;57(2):511-9.
RM PMID: 15697207
RT Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase.
RA Wise EL, Yew WS, Akana J, Gerlt JA, Rayment I
RL Biochemistry. 2005 Feb 15;44(6):1816-23.|
|Genome Property||GenProp0673: ribulose monophosphate pathway (HMM)|
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