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InterPro: IPR006383 HAD-superfamily hydrolase, subfamily IB, PSPase-like
Protein matches
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UniProtKB Matches: 2346 proteins |
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Accession
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IPR006383 HAD-SF_hydro_IB_PSP-like |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR004469 Phosphoserine phosphatase SerB
IPR006385 HAD-superfamily hydrolase, subfamily IB, PSPase-like, bacterial
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Found in
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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
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GO Term annotation
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Process
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GO:0008152 metabolic process
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Function
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GO:0016791 phosphatase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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.
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Structural links
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Database links
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Additional Reading
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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
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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
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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
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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
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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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