D00514
type: Enzyme
rlcp: p84
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/3.1.3.2
ec: https://purl.uniprot.org/enzyme/3.1.3.26
uniprot: P07102
kegg enzyme: acid phosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: acid phosphomonoesterase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: phosphomonoesterase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: glycerophosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: acid monophosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: acid phosphohydrolase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: acid phosphomonoester hydrolase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: uteroferrin
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: acid nucleoside diphosphate phosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: orthophosphoric-monoester phosphohydrolase (acid optimum)
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.2
kegg enzyme: 4-phytase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.26
kegg enzyme: 6-phytase (name based on 1L-numbering system and not 1D-numbering)
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.26
kegg enzyme: phytase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.26
kegg enzyme: phytate 6-phosphatase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.26
kegg enzyme: myo-inositol-hexakisphosphate 6-phosphohydrolase (name based on1L-numbering system and not 1D-numbering)
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/3.1.3.26
kegg pathway: gamma-Hexachlorocyclohexane degradation
kegg pathway: Inositol phosphate metabolism
kegg pathway: Riboflavin metabolism
kegg substrate: Orthophosphoric monoester
kegg substrate: myo-inositol hexakisphosphate
kegg substrate: H2O
kegg product: Alcohol
kegg product: 1D-myo-inositol 1,2,3,4,5-pentakisphosphate
kegg product: Orthophosphate
pdb: 1dklA01
pdb: 1dklB01
pdb: 1dkmA01
pdb: 1dknA01
pdb: 1dkoA01
pdb: 1dkpA01
pdb: 1dkqA01
pdb: 1dklA02
pdb: 1dklB02
pdb: 1dkmA02
pdb: 1dknA02
pdb: 1dkoA02
pdb: 1dkpA02
pdb: 1dkqA02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dklA01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dklB01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkmA01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dknA01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkoA01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkpA01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkqA01
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dklA02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dklB02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkmA02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dknA02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkoA02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkpA02
pdb bound state: Unbound
  compound: Orthophosphoric monoester
  pdb: 1dkqA02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dklA01
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dklB01
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dkmA01
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dknA01
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dkoA01
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dklA02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dklB02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dkmA02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dknA02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dkoA02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dkpA02
pdb bound state: Unbound
  compound: myo-inositol hexakisphosphate
  pdb: 1dkqA02
active site residues resources: Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site.
active site residues resources: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase.
references: Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
references: Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
references: Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site.
references: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase.
references: Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.
references: Crystal structures of Escherichia coli phytase and its complex with phytate.
references: Crystal structure of human prostatic acid phosphatase .
comment: According to the literature [2] and [3], His12 (of 1rpa/1rpt) acts as nucleophile, which attacks the phosphorous atom of the phosphate ester, whilst Asp258 protonates the leaving group. At the next stage, the deprotonated Asp258 abstracts proton from the water, which hydrolyzes the phosphorylated imidazole ring of His12 [2]. Moreover, the three positively charged arginine residues (Arg11, Arg15, Arg79) near His12 play an important role in the catalysis, as follows [2]; (1) The positive charged groups lower the pKa of the nucelophilic histidine (His12), so that the acidic phosphatase can function below pH 7. (2) These groups will orient the phosphate group in a proper position so that the nucleophilic attack at the phosphorous atom can take place while the phosphorous-oxygen bond is cleaved.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.1240
catalytic domain: index.html

gamma-Hexachlorocyclohexane degradation
type: KeggPathway
references: KEGG:MAP00361
ec: https://purl.uniprot.org/enzyme/3.1.3.2

Inositol phosphate metabolism
type: KeggPathway
references: KEGG:MAP00562
ec: https://purl.uniprot.org/enzyme/3.1.3.26

Riboflavin metabolism
type: KeggPathway
references: KEGG:MAP00740
ec: https://purl.uniprot.org/enzyme/3.1.3.2

Orthophosphoric monoester
type: KeggSubstrate
references: KEGG:C01153
ec: https://purl.uniprot.org/enzyme/3.1.3.2
compound type: carbohydrate
compound type: phosphate group/phosphate ion

myo-inositol hexakisphosphate
type: KeggSubstrate
references: KEGG:C01204
ec: https://purl.uniprot.org/enzyme/3.1.3.26
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:17401

H2O
type: KeggSubstrate
references: KEGG:C00001
ec: https://purl.uniprot.org/enzyme/3.1.3.2
ec: https://purl.uniprot.org/enzyme/3.1.3.26
compound type: H2O
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Alcohol
type: KeggProduct
references: KEGG:C00069
ec: https://purl.uniprot.org/enzyme/3.1.3.2
compound type: carbohydrate

1D-myo-inositol 1,2,3,4,5-pentakisphosphate
type: KeggProduct
references: KEGG:C04579
ec: https://purl.uniprot.org/enzyme/3.1.3.26
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:48405

Orthophosphate
type: KeggProduct
references: KEGG:C00009
ec: https://purl.uniprot.org/enzyme/3.1.3.2
ec: https://purl.uniprot.org/enzyme/3.1.3.26
compound type: phosphate group/phosphate ion
references: CHEBI:26078
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1dklA01
type: Pdb
references: 1dkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkl
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers);HIS 17;ASP 304

1dklB01
type: Pdb
references: 1dkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkl
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers);HIS 17;ASP 304

1dkmA01
type: Pdb
references: 1dkm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkm
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers);HIS 17;ASP 304

1dknA01
type: Pdb
references: 1dkn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkn
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers);HIS 17;ASP 304

1dkoA01
type: Pdb
references: 1dko
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dko
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers);HIS 17;ASP 304

1dkpA01
type: Pdb
references: 1dkp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkp
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers); ;ASP 304
comment: mutant H17A

1dkqA01
type: Pdb
references: 1dkq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dkq
catalytic residue: ARG 16;ARG 20;ARG 92;HIS 303(Stabilizers); ;ASP 304
comment: mutant H17A

Three-dimensional structure of rat acid phosphatase in complex with L(+)-tartrate.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8407898
journal: J Biol Chem
volume: 268
pages: 20744-6
published year: 1993
authors:
  item: Lindqvist Y
  item: Schneider G
  item: Vihko P
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/8168503
journal: Eur J Biochem
volume: 221
pages: 139-142
published year: 1994
authors:
  item: Lindqvist Y
  item: Schneider G
  item: Vihko P
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site.
type: BibliographicResource
comment: active site mutation, catalysis
references: http://www.ncbi.nlm.nih.gov/pubmed/8132635
journal: J Biol Chem
volume: 269
pages: 8971-8
published year: 1994
authors:
  item: Ostanin K
  item: Saeed A
  item: Van Etten RL

Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase.
type: BibliographicResource
comment: X-ray crystallography (2.9 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/9804805
journal: J Biol Chem
volume: 273
pages: 30406-9
published year: 1998
authors:
  item: LaCount MW
  item: Handy G
  item: Lebioda L
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.
type: BibliographicResource
comment: Improvement of catalytic efficiency by site-directed mutagenesis
references: http://www.ncbi.nlm.nih.gov/pubmed/11051103
journal: Arch Biochem Biophys
volume: 382
pages: 105-12
published year: 2000
authors:
  item: Rodriguez E
  item: Wood ZA
  item: Karplus PA
  item: Lei XG

Crystal structures of Escherichia coli phytase and its complex with phytate.
type: BibliographicResource
comment: X-ray crystallography (2.05 Angstroms)
medline id: 20122624
references: http://www.ncbi.nlm.nih.gov/pubmed/10655611
journal: Nat Struct Biol
volume: 7
pages: 108-13
published year: 2000
authors:
  item: Lim D
  item: Golovan S
  item: Forsberg CW
  item: Jia Z
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of human prostatic acid phosphatase .
type: BibliographicResource
comment: X-ray crystallography (3.1 Angstroms)
references: http://www.ncbi.nlm.nih.gov/pubmed/10639192
journal: Prostate
volume: 42
pages: 211-8
published year: 2000
authors:
  item: Jakob CG
  item: Lewinski K
  item: Kuciel R
  item: Ostrowski W
  item: Lebioda L

Analogue
compound: Orthophosphate
pdb: 1dkoA01
ligand het code: WO4

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.2, Fig.3, p.141-142
reference step: 3

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.4
reference step: 2

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.111