HMM Summary Page: TIGR00526

FunctionFolB domain
Trusted Cutoff45.05
Domain Trusted Cutoff45.05
Noise Cutoff35.65
Domain Noise Cutoff35.65
Isology Typedomain
HMM Length122
AuthorHaft DH
Entry DateOct 18 1999 5:03PM
Last ModifiedFeb 14 2011 3:27PM
CommentTwo 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.
ReferencesA2 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