HMM Summary Page: TIGR02137

Functionphosphoserine phosphatase/homoserine phosphotransferase bifunctional protein
Gene SymbolthrH
Trusted Cutoff223.40
Domain Trusted Cutoff223.40
Noise Cutoff77.65
Domain Noise Cutoff77.65
Isology Typeequivalog
EC Number3.1.3.3
HMM Length203
AuthorSelengut J
Entry DateMar 1 2004 3:14PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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).
ReferencesRN [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 PropertyGenProp0159: threonine biosynthesis from aspartate semialdehyde (HMM)