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

Protein matchesHelp
UniProtKB
Matches:
2346 proteins
AccessionHelp IPR006383 HAD-SF_hydro_IB_PSP-like
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR004469 Phosphoserine phosphatase SerB
IPR006385 HAD-superfamily hydrolase, subfamily IB, PSPase-like, bacterial
Found in IPR006384 Pyridoxal phosphate phosphatase-related
IPR006386 HAD-superfamily hydrolase, subfamily IB, PSPase-like, archaeal
IPR016965 Pyridoxal phosphate phosphatase, PHOSPHO2
IPR017718 HAD-superfamily hydrolase, subfamily IB, MtnX
GO Term annotationHelp
Process GO:0008152 metabolic process
Function GO:0016791 phosphatase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This group represents a subfamily of the haloacid dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included.

Structural linksHelp
Database linksHelp
Enzyme: EC:3.1.3

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR006383 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O82796 Phosphoserine phosphatase, chloroplastic

P42941 Phosphoserine phosphatase

P78330 Phosphoserine phosphatase

Q8R2H9 Phosphoethanolamine/phosphocholine 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
IPR016965 Pyridoxal phosphate phosphatase, PHOSPHO2
IPR006384 Pyridoxal phosphate phosphatase-related
SWISS-MODEL
PDB Chain
ModBase
CATH Domain
SCOP Domain

PublicationsHelp

Additional ReadingHelp
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
Xu Q, Saikatendu KS, Krishna SS, McMullan D, Abdubek P, Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Miller MD, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, Schwarzenbacher R, van den Bedem H, White A, Wolf G, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA.
Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 angstroms resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate.
Proteins 69 2007 433-9 [PubMed: 17654724]
http://dx.doi.org/10.1002/prot.21602
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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InterPro 24.0