Accession | TIGR02245 |
Name | HAD_IIID1 |
Function | HAD hydrolase, family IIID |
Trusted Cutoff | 192.25 |
Domain Trusted Cutoff | 192.25 |
Noise Cutoff | 130.25 |
Domain Noise Cutoff | 130.25 |
Isology Type | hypoth_equivalog |
HMM Length | 195 |
Author | Selengut J |
Entry Date | Jul 23 2004 2:43PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This 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]. |
References | RN [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 |