| Accession | TIGR02137 |
| Name | HSK-PSP |
| Function | phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein |
| Gene Symbol | thrH |
| Trusted Cutoff | 223.40 |
| Domain Trusted Cutoff | 223.40 |
| Noise Cutoff | 77.65 |
| Domain Noise Cutoff | 77.65 |
| Isology Type | equivalog |
| EC Number | 3.1.3.3 |
| HMM Length | 203 |
| Author | Selengut J |
| Entry Date | Mar 1 2004 3:14PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase [1]. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present.
This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain [2,3]. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338). |
| References | RN [1]
RM PMID: 14699121
RT The thrH gene product of pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity
RA Singh SK, Yang K, Subramanian K, Huynh T, Zhang X, Phillips MA, Zhang H
RL J Biol Chem. 2003 Dec 29 [Epub ahead of print]
RN [2]
RM PMID: 7966317
RT Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approac
h to database search.
RA Koonin EV, Tatusov RL.
RL J Mol Biol 1994 Nov 18;244(1):125-32
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 |
| Genome Property | GenProp0159: threonine biosynthesis from aspartate semialdehyde (HMM) |
