|Function||phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein|
|Domain Trusted Cutoff||223.40|
|Domain Noise Cutoff||77.65|
|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 . 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).|
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]
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
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)|
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