Accession | TIGR03128 |
Name | RuMP_HxlA |
Function | 3-hexulose-6-phosphate synthase |
Gene Symbol | hxlA |
Trusted Cutoff | 243.40 |
Domain Trusted Cutoff | 243.40 |
Noise Cutoff | 146.85 |
Domain Noise Cutoff | 146.85 |
Isology Type | equivalog_domain |
EC Number | 4.1.2.43 |
HMM Length | 206 |
Author | Haft DH |
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. |
References | RN [1]
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.
RN [2]
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) |