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CATH Superfamily 1.10.150.240

Putative phosphatase; domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Putative phosphatase; domain 2
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 23 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Phosphoglycolate phosphatase. [EC: 3.1.3.18]
2-phosphoglycolate + H(2)O = glycolate + phosphate.
    		 240 A0A023Z4J7 A0A025CQ34 A0A028AN79 A0A028E9S9 A0A069XPH2 A0A070FCV7 A0A070SN94 A0A070UX36 A0A080IHG7 A0A083ZBH7
    (230 more...)
    Phosphonoacetaldehyde hydrolase. [EC: 3.11.1.1]
    Phosphonoacetaldehyde + H(2)O = acetaldehyde + phosphate.
    • This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken.
    • The mechanism is similar to that used by EC 4.1.2.13 to break a C-C bond.
    		 225 A0A015QLK2 A0A015SLH3 A0A015T0R3 A0A015V4P3 A0A015VTC2 A0A015WEJ6 A0A015WSL1 A0A016ARR1 A0A016G5V0 A0A073I0I0
    (215 more...)
    Sorbitol-6-phosphatase. [EC: 3.1.3.50]
    Sorbitol 6-phosphate + H(2)O = sorbitol + phosphate.
    • Acts, very slowly, on hexose 6-phosphates.
    		 169 A0A023YY45 A0A025CQB8 A0A026UEB6 A0A028AK37 A0A028EBK9 A0A029HYJ3 A0A029IST8 A0A069XSL1 A0A069XTM7 A0A070EW16
    (159 more...)
    Mannitol-1-phosphatase. [EC: 3.1.3.22]
    D-mannitol 1-phosphate + H(2)O = D-mannitol + phosphate.
      		 169 A0A023YY45 A0A025CQB8 A0A026UEB6 A0A028AK37 A0A028EBK9 A0A029HYJ3 A0A029IST8 A0A069XSL1 A0A069XTM7 A0A070EW16
      (159 more...)
      Sugar-phosphatase. [EC: 3.1.3.23]
      Sugar phosphate + H(2)O = sugar + phosphate.
      • Has a wide specificity, acting on aldohexose 1-phosphates, ketohexose 1-phosphates, aldohexose 6-phosphates, ketohexose 6-phosphates, both phosphate ester bonds of fructose 1,6-bisphosphate, phosphoric esters of disaccharides, and on pentose and triose phosphates, but at a slower rate.
      		 169 A0A023YY45 A0A025CQB8 A0A026UEB6 A0A028AK37 A0A028EBK9 A0A029HYJ3 A0A029IST8 A0A069XSL1 A0A069XTM7 A0A070EW16
      (159 more...)
      2-deoxyglucose-6-phosphatase. [EC: 3.1.3.68]
      2-deoxy-D-glucose 6-phosphate + H(2)O = 2-deoxy-D-glucose + phosphate.
      • Also active toward fructose 1-phosphate.
      		 152 A0A023YY45 A0A025CQB8 A0A026UEB6 A0A028AK37 A0A028EBK9 A0A029HYJ3 A0A029IST8 A0A069XTM7 A0A070EW16 A0A070SS02
      (142 more...)
      Inorganic diphosphatase. [EC: 3.6.1.1]
      Diphosphate + H(2)O = 2 phosphate.
      • Specificity varies with the source and with the activating metal ion.
      • The enzyme from some sources may be identical with EC 3.1.3.1 or EC 3.1.3.9.
      • Cf. EC 7.1.3.1.
      		 137 A0A0B5NBX0 A0A0B8RB02 A0A0D0RJV4 A0A0D0RVH9 A0A0E0UZH9 A0A0E1Y2A5 A0A0F5RU90 A0A0F6J6X8 A0A0F7RAU2 A0A0H3GEW8
      (127 more...)
      Glucose-1-phosphatase. [EC: 3.1.3.10]
      Alpha-D-glucose 1-phosphate + H(2)O = D-glucose + phosphate.
      • Also acts, more slowly, on alpha-D-galactose 1-phosphate.
      		 49 A0A069XM74 A0A070FA37 A0A070SMY9 A0A073FNX5 A0A080FI36 A0A0A0F797 A0A0E0Y7J1 A0A0E1ST16 A0A0H7W2A4 A0A127GRY2
      (39 more...)
      Beta-phosphoglucomutase. [EC: 5.4.2.6]
      Beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate.
      • The enzyme is able to autophosphorylate itself with its substrate beta-D-glucose 1-phosphate.
      • Although this is a slow reaction, only a single turnover is required for activation.
      • Once the phosphorylated enzyme is formed, it generates the reaction intermediate beta-D-glucose 1,6-bisphosphate, which can be used to phosphorylate the enzyme in subsequent cycles.
      • Cf. EC 5.4.2.2.
      		 33 A0A069XKI4 A0A070SRX8 A0A070UZ79 A0A0A0FC68 A0A0E0TXK1 A0A0E1LWU5 A0A0E1T3D3 A0A164TV93 A0A1D8FMC6 A0A1X3IPG1
      (23 more...)
      5'-nucleotidase. [EC: 3.1.3.5]
      A 5'-ribonucleotide + H(2)O = a ribonucleoside + phosphate.
      • Wide specificity for 5'-nucleotides.
      		 21 A0A080ICF9 A0A0E2KWU4 A0A0F6CCV7 A0A0H3Q3G6 A0A0M7NIV8 A0A140NEG8 A0A1S9JEX0 A0A1X3L8S8 A0A1Z3UVL0 A0A3R0XS17
      (11 more...)
      (S)-2-haloacid dehalogenase. [EC: 3.8.1.2]
      (S)-2-haloacid + H(2)O = (R)-2-hydroxyacid + halide.
      • Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 (see also EC 3.8.1.9, EC 3.8.1.10 and EC 3.8.1.11).
      		 16 A0A0P0RIG8 A0A0P7DJX5 A0A1I0UVT9 A0A1T1HJY5 A0A2A3LWC1 A0A385CYX0 P24069 P24070 P60527 Q51645
      (6 more...)
      Glycerol-1-phosphatase. [EC: 3.1.3.21]
      Glycerol 1-phosphate + H(2)O = glycerol + phosphate.
      • The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate.
      • The enzyme from Saccharomyces cerevisiae also acts on propane-1,2- diol 1-phosphate, but not on a variety of other phosphate esters.
      		 12 A0A0L8VNP6 A0A0L8VRQ4 B5VHJ4 C7GTD0 C7GVY1 C8Z768 F4JTE7 N1P256 N1P561 P40106
      (2 more...)
      N-acetyl-D-muramate 6-phosphate phosphatase. [EC: 3.1.3.105]
      N-acetyl-D-muramate 6-phosphate + H(2)O = N-acetyl-D-muramate + phosphate.
      • The enzyme, characterized from Pseudomonas species, participates in a peptidoglycan salvage pathway.
      		 11 A0A0A7PY62 A0A179R8Y7 A0A2L0T2J0 A0A2L1IHS3 A0A2V3CSH6 A0A2V4FMY2 A0A355R982 A0A3A8C124 A0A495PM53 Q88M11
      (1 more...)
      5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase. [EC: 3.1.3.104]
      5-amino-6-(5-phospho-D-ribitylamino)uracil + H(2)O = 5-amino-6- (D-ribitylamino)uracil + phosphate.
      • The enzyme, which is found in plants and bacteria, is part of a pathway for riboflavin biosynthesis.
      • Most forms of the enzyme has a broad substrate specificity.
      		 6 A0A139KAY1 A0A1H8FVR5 D7IDL1 F4JTE7 Q8A947 Q9LDD5
      Lipid-phosphate phosphatase. [EC: 3.1.3.76]
      (9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O = (9S,10S)- 9,10-dihydroxyoctadecanoate + phosphate.
      • The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10.
      • The best substrates for this enzyme are 10-hydroxy-9- (phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form.
      • The phosphatase activity is not found in plant EC 3.3.2.10 or in mammalian EC 3.3.2.9.
      		 5 A0A480V3S2 P34913 P34914 P80299 Q6Q2C2
      Soluble epoxide hydrolase. [EC: 3.3.2.10]
      An epoxide + H(2)O = a glycol.
      • Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism.
      • It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides.
      • The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76.
      • Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate.
      • The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product.
      • Formerly EC 3.3.2.3, EC 4.2.1.63 and EC 4.2.1.64.
      		 5 A0A480V3S2 P34913 P34914 P80299 Q6Q2C2
      Pseudouridine 5'-phosphatase. [EC: 3.1.3.96]
      Pseudouridine 5'-phosphate + H(2)O = pseudouridine + phosphate.
      • The enzyme, isolated from animals, dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation.
      • Formerly EC 3.1.3.n6.
      		 3 Q08623 Q94529 Q9D5U5
      Haloacetate dehalogenase. [EC: 3.8.1.3]
      Haloacetate + H(2)O = glycolate + halide.
        		 2 Q01399 Q7DI63
        FMN hydrolase. [EC: 3.1.3.102]
        FMN + H(2)O = riboflavin + phosphate.
        • The enzyme, found in many isoforms purified from both bacteria and plants, is a member of the haloacid dehalogenase superfamily.
        • Most of the isoforms have a wide substrate specificity, but isoforms specific for FMN also exist.
        		 2 A0A178V341 Q84MD8
        Riboflavin kinase. [EC: 2.7.1.26]
        ATP + riboflavin = ADP + FMN.
        • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B(6), vitamin B12 and folates.
        • While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2.
        • In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP.
        		 2 A0A178V341 Q84MD8
        2-aminoethylphosphonate--pyruvate transaminase. [EC: 2.6.1.37]
        (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine.
        • 2-aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
        		 2 A0A488X0G3 Q183T0
        Imidazoleglycerol-phosphate dehydratase. [EC: 4.2.1.19]
        D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2- oxopropyl phosphate + H(2)O.
          		 1 P28624
          Validoxylamine A 7'-phosphate phosphatase. [EC: 3.1.3.101]
          Validoxylamine A 7'-phosphate + H(2)O = validoxylamine A + phosphate.
          • The enzyme, characterized from the bacterium Streptomyces hygroscopicus subsp. limoneus, is involved in the biosynthesis of the antifungal agent validamycin A.
          		 1 Q15JF8