HMM Summary Page: TIGR02245

FunctionHAD hydrolase, family IIID
Trusted Cutoff192.25
Domain Trusted Cutoff192.25
Noise Cutoff130.25
Domain Noise Cutoff130.25
Isology Typehypoth_equivalog
HMM Length195
AuthorSelengut J
Entry DateJul 23 2004 2:43PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains [1], in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain [2] between motifs 1 and 2 or between 2 and 3, it is formally a "class III" HAD [3].
ReferencesRN [1] RM PMID: 7966317 RT Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search. RA Koonin EV, Tatusov RL. RL J Mol Biol 1994 Nov 18;244(1):125-32 RN [2] RM PMID: 10956028 RT The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. RA Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN. RL Biochemistry 2000 Aug 29;39(34):10385-96 RN [3] RM PMID: 11601995 RT MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases. RA Selengut, JD RL Biochemistry 2001 Oct 23;40(42):12704-11