HMM Summary Page: TIGR00526
Accession | TIGR00526 |
Name | folB_dom |
Function | FolB domain |
Trusted Cutoff | 45.05 |
Domain Trusted Cutoff | 45.05 |
Noise Cutoff | 35.65 |
Domain Noise Cutoff | 35.65 |
Isology Type | domain |
HMM Length | 122 |
Author | Haft DH |
Entry Date | Oct 18 1999 5:03PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Two paralogous genes of E. coli, folB (dihydroneopterin aldolase) and folX (d-erythro-7,8-dihydroneopterin triphosphate epimerase) are homologous to each other and homo-octameric. In Pneumocystis carinii, a multifunctional enzyme of folate synthesis has an N-terminal region active as dihydroneopterin aldolase. This region consists of two tandem sequences each homologous to folB and forms tetramers. |
References | A2 hmmalign AL Clustalw RN [1] RM 98316300 RT Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. RA Haussmann C, Rohdich F, Schmidt E, Bacher A, Richter G RL J Biol Chem 1998 Jul 10;273(28):17418-24 RN [2] RM 98376447 RT Single amino acid substitutions disrupt tetramer formation in the dihydroneopterin aldolase enzyme of Pneumocystis carinii. RA Thomas MC, Ballantine SP, Bethell SS, Bains S, Kellam P, Delves CJ RL Biochemistry 1998 Aug 18;37(33):11629-36 |