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InterPro: IPR004469 Phosphoserine phosphatase SerB

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UniProtKB

Matches:

1078 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004469 SerB

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00338	serB	1078
Signatures in BioMart

InterPro Relationships Help

Parent

IPR006383 HAD-superfamily hydrolase, subfamily IB, PSPase-like

GO Term annotation Help

Process

GO:0006564 L-serine biosynthetic process

Function

GO:0004647 phosphoserine phosphatase activity

InterPro annotation

Entry Details in BioMart

Abstract

Phosphoserine phosphatase (SerB), (EC:3.1.3.3), also known as O-phosphoserine phosphohydrolase, is involved in both serine and glycine biosynthesis. It catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate, which is the last step in the biosynthesis of serine from carbohydrates. The reaction proceeds via the formation of a phosphoryl-enzyme intermediate. It acts as a homodimer, and requires magnesium as a cofactor.

Structural links Help

PDB - click here

SCOP: c.108.1.4

CATH: 1.10.150.210 , 3.40.50.1000

Database links Help

Enzyme: EC:3.1.3.3

CluSTr: ALLvsALL:26689:40.2

PRIAM: PRI001266

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004469

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O82796 Phosphoserine phosphatase, chloroplastic

P42941 Phosphoserine phosphatase

P78330 Phosphoserine phosphatase

Q99LS3 Phosphoserine phosphatase

Q9VSY6 Phosphoserine phosphatase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005834	Haloacid dehalogenase-like hydrolase
IPR004469	Phosphoserine phosphatase SerB
IPR006383	HAD-superfamily hydrolase, subfamily IB, PSPase-like
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Kim HY, Heo YS, Kim JH, Park MH, Moon J, Kim E, Kwon D, Yoon J, Shin D, Jeong EJ, Park SY, Lee TG, Jeon YH, Ro S, Cho JM, Hwang KY. Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase. J. Biol. Chem. 277 2002 46651-8 [PubMed: 12213811] http://dx.doi.org/10.1074/jbc.M204866200
	Cho H, Wang W, Kim R, Yokota H, Damo S, Kim SH, Wemmer D, Kustu S, Yan D. BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase. Proc. Natl. Acad. Sci. U.S.A. 98 2001 8525-30 [PubMed: 11438683] http://dx.doi.org/10.1073/pnas.131213698
	Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C. High-resolution structure of human phosphoserine phosphatase in open conformation. Acta Crystallogr. D Biol. Crystallogr. 59 2003 971-7 [PubMed: 12777757] http://dx.doi.org/10.1107/S0907444903005407
	Wang W, Kim R, Jancarik J, Yokota H, Kim SH. Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution. Structure 9 2001 65-71 [PubMed: 11342136] http://dx.doi.org/10.1016/S0969-2126(00)00558-X
	Wang W, Cho HS, Kim R, Jancarik J, Yokota H, Nguyen HH, Grigoriev IV, Wemmer DE, Kim SH. Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states. J. Mol. Biol. 319 2002 421-31 [PubMed: 12051918] http://dx.doi.org/10.1016/S0022-2836(02)00324-8

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