Table 1 The principal known or reliably inferred molecular functions of histidine phosphatase domains grouped into broad functional categories

Detail on reactions catalysed, their broader significance and further references can be found in Supplementary Table S2 (http://www.BiochemJ.org/bj/409/bj4090333add.htm) and in the text.

BranchBroad functional categoryProtein and key molecular function referenceExample speciesEC number
1CatalyticIntermediary metabolismdPGM [4]E. coli, S. cerevisiae, human5.4.2.1 (also 3.1.3.13 and 5.4.2.4)
BPGM [120]Human5.4.2.4 (also 5.4.2.1 and 3.1.3.13)
α-Ribazole phosphatase (CobC) [16]Salmonella Typhimurium3.1.3.73
Mannitol-1-phosphatase [79]Eimeria tenella3.1.3.22
Neo13 [18]Streptomyces fradiae3.1.3.-
Metabolic regulationPFK2/F26BPase [121]Eukaryotes3.1.3.46
TIGAR [28]Eukaryotes3.1.3.46
Other regulatory or developmental processSixA [15]E. coli3.1.3.-
EPP [19]Bombyx mori, Drosophila melanogaster3.1.3.-
Sts-1, Sts-2 (also known as UBASH3A, TULA) [20]Human3.1.3.-
PMU1 [8]S. cerevisiae3.1.3.-
UnknownPhoE [116]G. stearothermophilus3.1.3.-
Non-catalyticTFIIIC τ 55 kDa subunit [39]S. cerevisiae
(?)
PGAM5 [38]Human
2CatalyticExtracellular metabolism/scavengingPho5p [22]S. cerevisiaeMay include 3.6.1.3
Glucose-1-phosphatase [21]E. coli3.1.3.10
Phytase [23]Aspergilli and E. coli3.1.3.8, 3.1.3.26
Regulation of signalling molecule concentrationMinpp1 [122]Human3.1.3.62
Lysophosphatidic acid phosphatase [30]Human3.1.3.2
Other regulatory or developmental processPAP [123]Human3.1.3.48
Testicular acid phosphatase [34]Human3.1.3.48
Lysosomal acid phosphatase (LAP) and Acp5/TRAP [36]Human?
Peripheral vacuolar acid phosphatase [37]Giardia lamblia?