PPA_ECOLI
ID PPA_ECOLI Reviewed; 432 AA.
AC P07102;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Phytase AppA {ECO:0000303|PubMed:30712472};
DE EC=3.1.3.- {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:30712472, ECO:0000269|PubMed:8387749, ECO:0000269|Ref.8};
DE AltName: Full=6-phytase {ECO:0000303|PubMed:11035187, ECO:0000303|PubMed:8387749};
DE AltName: Full=Histidine acid phosphatase phytase {ECO:0000303|PubMed:30712472};
DE Short=HAP phytase {ECO:0000303|PubMed:30712472};
DE AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase {ECO:0000303|PubMed:11035187};
DE AltName: Full=Phosphoanhydride phosphatase {ECO:0000303|PubMed:6282821};
DE EC=3.6.1.- {ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8407904};
DE AltName: Full=pH 2.5 acid phosphatase {ECO:0000303|PubMed:6282821};
DE Short=Acid phosphatase {ECO:0000303|PubMed:1429631, ECO:0000303|PubMed:6282821};
DE EC=3.1.3.- {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8387749, ECO:0000269|PubMed:8407904, ECO:0000269|Ref.8};
DE Flags: Precursor;
GN Name=appA {ECO:0000303|PubMed:3038201}; OrderedLocusNames=b0980, JW0963;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-29.
RC STRAIN=K12;
RX PubMed=2168385; DOI=10.1128/jb.172.9.5497-5500.1990;
RA Dassa J., Marck C., Boquet P.L.;
RT "The complete nucleotide sequence of the Escherichia coli gene appA reveals
RT significant homology between pH 2.5 acid phosphatase and glucose-1-
RT phosphatase.";
RL J. Bacteriol. 172:5497-5500(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112, AND TRANSCRIPTIONAL REGULATION
RP BY CAMP.
RX PubMed=3038201; DOI=10.1016/0300-9084(87)90045-9;
RA Touati E., Danchin A.;
RT "The structure of the promoter and amino terminal region of the pH 2.5 acid
RT phosphatase structural gene (appA) of E. coli: a negative control of
RT transcription mediated by cyclic AMP.";
RL Biochimie 69:215-221(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=K12;
RX PubMed=1658595; DOI=10.1007/bf00267454;
RA Dassa J., Fsihi H., Marck C., Dion M., Kieffer-Bontemps M., Boquet P.L.;
RT "A new oxygen-regulated operon in Escherichia coli comprises the genes for
RT a putative third cytochrome oxidase and for pH 2.5 acid phosphatase
RT (appA).";
RL Mol. Gen. Genet. 229:341-352(1991).
RN [7]
RP PROTEIN SEQUENCE OF 23-35, FUNCTION AS A PHYTASE, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=8387749; DOI=10.1006/abbi.1993.1261;
RA Greiner R., Konietzny U., Jany K.-D.;
RT "Purification and characterization of two phytases from Escherichia coli.";
RL Arch. Biochem. Biophys. 303:107-113(1993).
RN [8]
RP PROTEIN SEQUENCE OF 23-33, FUNCTION AS A PHYTASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RA Greiner R., Jany K.-D.;
RT "Characterization of a phytase from Escherichia coli.";
RL Biol. Chem. Hoppe-Seyler 372:664-665(1991).
RN [9]
RP FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=6282821; DOI=10.1016/s0021-9258(18)34481-8;
RA Dassa E., Cahu M., Desjoyaux-Cherel B., Boquet P.L.;
RT "The acid phosphatase with optimum pH of 2.5 of Escherichia coli.
RT Physiological and Biochemical study.";
RL J. Biol. Chem. 257:6669-6676(1982).
RN [10]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF ARG-38; HIS-39; ARG-42; ARG-85; ARG-114 AND HIS-325, AND ACTIVE SITE.
RX PubMed=1429631; DOI=10.1016/s0021-9258(18)50022-3;
RA Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M., van Etten R.L.;
RT "Overexpression, site-directed mutagenesis, and mechanism of Escherichia
RT coli acid phosphatase.";
RL J. Biol. Chem. 267:22830-22836(1992).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-326, AND ACTIVE SITE.
RX PubMed=8407904; DOI=10.1016/s0021-9258(19)36851-6;
RA Ostanin K., Van Etten R.L.;
RT "Asp304 of Escherichia coli acid phosphatase is involved in leaving group
RT protonation.";
RL J. Biol. Chem. 268:20778-20784(1993).
RN [12]
RP INDUCTION.
RX PubMed=8071219; DOI=10.1128/jb.176.17.5414-5422.1994;
RA Atlung T., Brondsted L.;
RT "Role of the transcriptional activator AppY in regulation of the cyx appA
RT operon of Escherichia coli by anaerobiosis, phosphate starvation, and
RT growth phase.";
RL J. Bacteriol. 176:5414-5422(1994).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND BIOTECHNOLOGY.
RX PubMed=10696472; DOI=10.1139/cjm-46-1-59;
RA Golovan S., Wang G., Zhang J., Forsberg C.W.;
RT "Characterization and overproduction of the Escherichia coli appA encoded
RT bifunctional enzyme that exhibits both phytase and acid phosphatase
RT activities.";
RL Can. J. Microbiol. 46:59-71(2000).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11035187; DOI=10.1016/s0168-1656(00)00331-x;
RA Greiner R., Carlsson N., Alminger M.L.;
RT "Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a
RT phytate-degrading enzyme of Escherichia coli.";
RL J. Biotechnol. 84:53-62(2001).
RN [15]
RP ACTIVITY REGULATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-99; CYS-130;
RP CYS-155; CYS-200; CYS-210; CYS-404; CYS-413 AND CYS-430.
RX PubMed=15642731; DOI=10.1074/jbc.m411774200;
RA Berkmen M., Boyd D., Beckwith J.;
RT "The nonconsecutive disulfide bond of Escherichia coli phytase (AppA)
RT renders it dependent on the protein-disulfide isomerase, DsbC.";
RL J. Biol. Chem. 280:11387-11394(2005).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-38; HIS-39; GLY-40;
RP VAL-41; ARG-42; ALA-43; PRO-44; THR-45; LYS-46; ALA-47 AND THR-48.
RX PubMed=30712472; DOI=10.1080/09168451.2019.1571897;
RA Wada M., Hayashi Y., Arai M.;
RT "Mutational analysis of a catalytically important loop containing active
RT site and substrate-binding site in Escherichia coli phytase AppA.";
RL Biosci. Biotechnol. Biochem. 83:860-868(2019).
RN [17] {ECO:0007744|PDB:1DKL, ECO:0007744|PDB:1DKM, ECO:0007744|PDB:1DKN, ECO:0007744|PDB:1DKO, ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP PHYTATE, SUBUNIT, MUTAGENESIS OF HIS-39, ACTIVE SITES, AND DISULFIDE BOND.
RX PubMed=10655611; DOI=10.1038/72371;
RA Lim D., Golovan S., Forsberg C.W., Jia Z.;
RT "Crystal structures of Escherichia coli phytase and its complex with
RT phytate.";
RL Nat. Struct. Biol. 7:108-113(2000).
RN [18] {ECO:0007744|PDB:4TSR}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 23-432 IN COMPLEX WITH
RP D-MYO-INOSITOL-HEXASULPHATE, AND DISULFIDE BOND.
RA Wu T.H., Chen C.C., Huang C.H., Guo R.T.;
RT "The Complex Structure of mutant Phytase with IHS.";
RL Submitted (JUN-2014) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolysis of phytate (or myo-inositol
CC hexakisphosphate, an indigestible organic form of phosphorus that is
CC found in many plant tissues) to myo-inositol and inorganic phosphate
CC (PubMed:8387749, Ref.8, PubMed:10696472, PubMed:11035187,
CC PubMed:30712472). Dephosphorylates phytate in a stereospecific way by
CC sequential removal of phosphate groups to produce myo-inositol 2-
CC monophosphate (PubMed:11035187). Also shows phosphoanhydride
CC phosphatase activity and hydrolyzes the distal phosphoryl residues of
CC GTP, the 5'-beta-phosphoryl residue of the regulatory nucleotide ppGpp
CC and tripolyphosphates (PubMed:6282821, PubMed:1429631, PubMed:8407904).
CC Does not split most phosphomonoesters with the exception of the
CC synthetic substrate p-nitrophenyl phosphate (pNPP), 2,3-
CC bisphosphoglycerate and fructose 1,6-bisphosphate (PubMed:6282821,
CC Ref.8, PubMed:1429631, PubMed:8387749, PubMed:8407904,
CC PubMed:10696472). {ECO:0000269|PubMed:10696472,
CC ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:1429631,
CC ECO:0000269|PubMed:30712472, ECO:0000269|PubMed:6282821,
CC ECO:0000269|PubMed:8387749, ECO:0000269|PubMed:8407904,
CC ECO:0000269|Ref.8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC 1,2,3,4,5-pentakisphosphate + phosphate; Xref=Rhea:RHEA:68308,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130,
CC ChEBI:CHEBI:177294; Evidence={ECO:0000269|PubMed:10696472,
CC ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:30712472,
CC ECO:0000269|PubMed:8387749, ECO:0000269|Ref.8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68309;
CC Evidence={ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:11035187,
CC ECO:0000269|PubMed:30712472, ECO:0000269|PubMed:8387749,
CC ECO:0000269|Ref.8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,2,3,4,5-pentakisphosphate + H2O = 1D-myo-
CC inositol 2,3,4,5-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:68312,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177294,
CC ChEBI:CHEBI:177295; Evidence={ECO:0000269|PubMed:11035187,
CC ECO:0000269|PubMed:8387749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68313;
CC Evidence={ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:8387749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 2,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 2,4,5-triphosphate + phosphate; Xref=Rhea:RHEA:68316,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177295,
CC ChEBI:CHEBI:177296; Evidence={ECO:0000269|PubMed:11035187,
CC ECO:0000269|PubMed:8387749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68317;
CC Evidence={ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:8387749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 2,4,5-triphosphate + H2O = 1D-myo-inositol
CC 2,5-bisphosphate + phosphate; Xref=Rhea:RHEA:68320,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177296,
CC ChEBI:CHEBI:177297; Evidence={ECO:0000269|PubMed:11035187};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68321;
CC Evidence={ECO:0000269|PubMed:11035187};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 2,5-bisphosphate + H2O = 1D-myo-inositol 2-
CC phosphate + phosphate; Xref=Rhea:RHEA:68324, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:177297;
CC Evidence={ECO:0000269|PubMed:11035187};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68325;
CC Evidence={ECO:0000269|PubMed:11035187};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:6282821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000269|PubMed:6282821};
CC -!- ACTIVITY REGULATION: Contains three consecutive and one non-consecutive
CC disulfide bonds and shows a strong dependence on DsbC for its full
CC activity (PubMed:15642731). Competitively inhibited by tartaric acid
CC and by sodium fluorid (PubMed:6282821, PubMed:8387749).
CC {ECO:0000269|PubMed:15642731, ECO:0000269|PubMed:6282821,
CC ECO:0000269|PubMed:8387749}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 mM for phytate {ECO:0000269|Ref.8};
CC KM=0.63 mM for phytate {ECO:0000269|PubMed:10696472};
CC KM=15 uM for D-Ins(1,2,3,4,5)P5 {ECO:0000269|PubMed:11035187};
CC KM=0.35 mM for GTP {ECO:0000269|PubMed:6282821};
CC KM=1.8 mM for ppGpp {ECO:0000269|PubMed:6282821};
CC KM=0.15 mM for tripolyphosphate {ECO:0000269|PubMed:1429631};
CC KM=6.5 mM for GDP {ECO:0000269|PubMed:6282821};
CC KM=20 mM for ATP {ECO:0000269|PubMed:6282821};
CC KM=2.77 mM for pNPP {ECO:0000269|PubMed:6282821};
CC KM=2.6 mM for pNPP {ECO:0000269|Ref.8};
CC KM=2.8 mM for pNPP {ECO:0000269|PubMed:1429631};
CC KM=5 mM for 2,3-bisphosphoglycerate {ECO:0000269|PubMed:6282821};
CC KM=5 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:6282821};
CC KM=3.0 mM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:1429631};
CC Vmax=2326 umol/min/mg enzyme with phytate as substrate
CC {ECO:0000269|PubMed:10696472};
CC Vmax=9235 umol/min/mg enzyme with D-Ins(1,2,3,4,5)P5 as substrate
CC {ECO:0000269|PubMed:11035187};
CC Vmax=22 nmol/min/mg enzyme with GTP as substrate
CC {ECO:0000269|PubMed:6282821};
CC Vmax=40 nmol/min/mg enzyme with ppGpp as substrate
CC {ECO:0000269|PubMed:6282821};
CC Vmax=440 umol/min/mg enzyme with tripolyphosphate as substrate
CC {ECO:0000269|PubMed:1429631};
CC Vmax=5 nmol/min/mg enzyme with GDP as substrate
CC {ECO:0000269|PubMed:6282821};
CC Vmax=62 nmol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:6282821};
CC Vmax=208 nmol/min/mg enzyme with pNPP as substrate
CC {ECO:0000269|PubMed:6282821};
CC Vmax=530 umol/min/mg enzyme with pNPP as substrate
CC {ECO:0000269|PubMed:1429631};
CC Vmax=625 nmol/min/mg enzyme with 2,3-bisphosphoglycerate as substrate
CC {ECO:0000269|PubMed:6282821};
CC Vmax=384 nmol/min/mg enzyme with fructose 1,6-bisphosphate as
CC substrate {ECO:0000269|PubMed:6282821};
CC Vmax=764 umol/min/mg enzyme with fructose 1,6-bisphosphate as
CC substrate {ECO:0000269|PubMed:1429631};
CC pH dependence:
CC Optimum pH is 4.5 for phytase activity (PubMed:8387749,
CC PubMed:10696472). Optimum pH is 2.5 for acid phosphatase activity
CC (PubMed:6282821). Optimum pH is 2.5-3.0 for acid phosphatase activity
CC (PubMed:10696472). {ECO:0000269|PubMed:10696472,
CC ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8387749};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius for phytase activity
CC (PubMed:8387749). Optimum temperature is 60 degrees Celsius for
CC phytase activity (PubMed:10696472). {ECO:0000269|PubMed:10696472,
CC ECO:0000269|PubMed:8387749};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10655611,
CC ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8387749,
CC ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10696472,
CC ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:8387749,
CC ECO:0000269|PubMed:8407904}.
CC -!- INDUCTION: Induced by phosphate starvation, anaerobiosis and entry into
CC stationary phase (PubMed:6282821, PubMed:8387749, PubMed:8071219).
CC Regulated by the HTH-type transcriptional regulator AppY
CC (PubMed:8071219). Negatively controlled by the cAMP-cAMP receptor (CAP)
CC complex (PubMed:6282821, PubMed:3038201). {ECO:0000269|PubMed:3038201,
CC ECO:0000269|PubMed:6282821, ECO:0000269|PubMed:8071219,
CC ECO:0000269|PubMed:8387749}.
CC -!- BIOTECHNOLOGY: The properties of the phytase including the low pH
CC optimum, protease resistance and high activity, demonstrate that the
CC enzyme is a good candidate for industrial production as a feed enzyme
CC and is therefore of potential commercial interest.
CC {ECO:0000269|PubMed:10696472}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M58708; AAA72086.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74065.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35745.1; -; Genomic_DNA.
DR EMBL; X05471; CAA29031.1; -; Genomic_DNA.
DR EMBL; S63811; AAB20286.1; -; Genomic_DNA.
DR PIR; B36733; B36733.
DR RefSeq; NP_415500.1; NC_000913.3.
DR RefSeq; WP_001300464.1; NZ_SSZK01000002.1.
DR PDB; 1DKL; X-ray; 2.30 A; A/B=23-432.
DR PDB; 1DKM; X-ray; 2.25 A; A=23-432.
DR PDB; 1DKN; X-ray; 2.40 A; A=23-432.
DR PDB; 1DKO; X-ray; 2.38 A; A=23-432.
DR PDB; 1DKP; X-ray; 2.28 A; A=23-432.
DR PDB; 1DKQ; X-ray; 2.05 A; A=23-432.
DR PDB; 4TSR; X-ray; 2.07 A; A=23-432.
DR PDBsum; 1DKL; -.
DR PDBsum; 1DKM; -.
DR PDBsum; 1DKN; -.
DR PDBsum; 1DKO; -.
DR PDBsum; 1DKP; -.
DR PDBsum; 1DKQ; -.
DR PDBsum; 4TSR; -.
DR AlphaFoldDB; P07102; -.
DR SMR; P07102; -.
DR BioGRID; 4259354; 22.
DR IntAct; P07102; 3.
DR STRING; 511145.b0980; -.
DR SWISS-2DPAGE; P07102; -.
DR jPOST; P07102; -.
DR PaxDb; P07102; -.
DR PRIDE; P07102; -.
DR EnsemblBacteria; AAC74065; AAC74065; b0980.
DR EnsemblBacteria; BAA35745; BAA35745; BAA35745.
DR GeneID; 946206; -.
DR KEGG; ecj:JW0963; -.
DR KEGG; eco:b0980; -.
DR PATRIC; fig|1411691.4.peg.1293; -.
DR EchoBASE; EB0047; -.
DR eggNOG; ENOG502Z7K9; Bacteria.
DR HOGENOM; CLU_030561_3_0_6; -.
DR InParanoid; P07102; -.
DR OMA; YVAHDTN; -.
DR PhylomeDB; P07102; -.
DR BioCyc; EcoCyc:APPA-MON; -.
DR BioCyc; MetaCyc:APPA-MON; -.
DR BRENDA; 3.1.3.26; 2026.
DR EvolutionaryTrace; P07102; -.
DR PRO; PR:P07102; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0008707; F:4-phytase activity; IEA:UniProtKB-EC.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; IDA:EcoCyc.
DR GO; GO:0008252; F:nucleotidase activity; IDA:EcoCyc.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0071454; P:cellular response to anoxia; IDA:EcoCyc.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IDA:EcoCyc.
DR GO; GO:0016311; P:dephosphorylation; IDA:EcoCyc.
DR GO; GO:0033518; P:myo-inositol hexakisphosphate dephosphorylation; IDA:EcoCyc.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 2.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2168385,
FT ECO:0000269|PubMed:8387749, ECO:0000269|Ref.8"
FT CHAIN 23..432
FT /note="Phytase AppA"
FT /id="PRO_0000023947"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:10655611,
FT ECO:0000305|PubMed:1429631"
FT ACT_SITE 326
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:10655611,
FT ECO:0000305|PubMed:8407904"
FT BINDING 38
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18,
FT ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ"
FT BINDING 42..46
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18,
FT ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ"
FT BINDING 114
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18,
FT ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ"
FT BINDING 289
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:10655611,
FT ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ"
FT BINDING 325..327
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:10655611, ECO:0000305|Ref.18,
FT ECO:0007744|PDB:1DKP, ECO:0007744|PDB:1DKQ"
FT DISULFID 99..130
FT /evidence="ECO:0000269|PubMed:10655611,
FT ECO:0000269|PubMed:15642731, ECO:0000269|Ref.18"
FT DISULFID 155..430
FT /evidence="ECO:0000269|PubMed:10655611,
FT ECO:0000269|PubMed:15642731, ECO:0000269|Ref.18"
FT DISULFID 200..210
FT /evidence="ECO:0000269|PubMed:10655611,
FT ECO:0000269|PubMed:15642731"
FT DISULFID 404..413
FT /evidence="ECO:0000269|PubMed:10655611,
FT ECO:0000269|PubMed:15642731, ECO:0000269|Ref.18"
FT MUTAGEN 38
FT /note="R->A: Loss of activity with pNPP and phytate as
FT substrates."
FT /evidence="ECO:0000269|PubMed:1429631,
FT ECO:0000269|PubMed:30712472"
FT MUTAGEN 38
FT /note="R->G: Loss of activity with phytate as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 39
FT /note="H->A,G: Loss of activity with phytate as substrate."
FT /evidence="ECO:0000269|PubMed:10655611,
FT ECO:0000269|PubMed:30712472"
FT MUTAGEN 39
FT /note="H->N: Loss of activity with pNPP as substrate."
FT /evidence="ECO:0000269|PubMed:1429631"
FT MUTAGEN 40
FT /note="G->A: Retains 50% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 41
FT /note="V->A: Retains 70% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 41
FT /note="V->G: Retains less than 10% of wild-type activity
FT with phytate as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 42
FT /note="R->A: Shows residual activity with pNPP as
FT substrate. Loss of activity with phytate as substrate."
FT /evidence="ECO:0000269|PubMed:1429631,
FT ECO:0000269|PubMed:30712472"
FT MUTAGEN 42
FT /note="R->G: Loss of activity with phytate as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 43
FT /note="A->G: Retains 70% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 44
FT /note="P->A: Retains 70% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 44
FT /note="P->G: Retains 50% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 45
FT /note="T->A: Retains 20% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 45
FT /note="T->G: Retains less than 10% of wild-type activity
FT with phytate as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 46
FT /note="K->A,G: Retains 40% of wild-type activity with
FT phytate as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 47
FT /note="A->G: Retains 80% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 48
FT /note="T->A: Retains 80% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 48
FT /note="T->G: Retains 90% of wild-type activity with phytate
FT as substrate."
FT /evidence="ECO:0000269|PubMed:30712472"
FT MUTAGEN 85
FT /note="R->A: Does not affect activity with pNPP as
FT substrate."
FT /evidence="ECO:0000269|PubMed:1429631"
FT MUTAGEN 99
FT /note="C->S: Retains less than 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 114
FT /note="R->A: Shows residual activity with pNPP as
FT substrate."
FT /evidence="ECO:0000269|PubMed:1429631"
FT MUTAGEN 130
FT /note="C->S: Retains less than 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 155
FT /note="C->S: Retains less than 10% of wild-type activity.
FT Does not require DsbC for its remaining activity; when
FT associated with S-430."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 200
FT /note="C->S: Retains 70% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 210
FT /note="C->S: Retains 35% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 325
FT /note="H->A: Shows residual activity with pNPP as
FT substrate."
FT /evidence="ECO:0000269|PubMed:1429631"
FT MUTAGEN 326
FT /note="D->A: 28-fold decrease in Vmax with pNPP as
FT substrate. 1600-fold decrease in Vmax with fructose 1,6-
FT bisphosphate as substrate. Does not affect the Km values of
FT the substrates pNPP, fructose 1,6-diphosphate and
FT tripolyphosphate."
FT /evidence="ECO:0000269|PubMed:8407904"
FT MUTAGEN 326
FT /note="D->E: 40-fold decrease in Vmax with pNPP as
FT substrate. 460-fold decrease in Vmax with fructose 1,6-
FT bisphosphate as substrate. Does not affect the Km values of
FT the substrates pNPP, fructose 1,6-diphosphate and
FT tripolyphosphate."
FT /evidence="ECO:0000269|PubMed:8407904"
FT MUTAGEN 404
FT /note="C->S: Retains less than 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 413
FT /note="C->S: Retains less than 10% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:15642731"
FT MUTAGEN 430
FT /note="C->S: Retains less than 10% of wild-type activity.
FT Does not require DsbC for its remaining activity; when
FT associated with S-155."
FT /evidence="ECO:0000269|PubMed:15642731"
FT CONFLICT 51..66
FT /note="MQDVTPDAWPTWPVKL -> NAGCHPRRMANLAGKT (in Ref. 5;
FT CAA29031)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..76
FT /note="EL -> DV (in Ref. 5; CAA29031)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="D -> S (in Ref. 5; CAA29031)"
FT /evidence="ECO:0000305"
FT STRAND 27..38
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4TSR"
FT HELIX 71..90
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1DKQ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1DKQ"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1DKQ"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1DKQ"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:1DKN"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 232..249
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 262..279
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:1DKQ"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 367..376
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:1DKQ"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:4TSR"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:1DKQ"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:1DKQ"
SQ SEQUENCE 432 AA; 47057 MW; 6510C6C579177F11 CRC64;
MKAILIPFLS LLIPLTPQSA FAQSEPELKL ESVVIVSRHG VRAPTKATQL MQDVTPDAWP
TWPVKLGWLT PRGGELIAYL GHYQRQRLVA DGLLAKKGCP QSGQVAIIAD VDERTRKTGE
AFAAGLAPDC AITVHTQADT SSPDPLFNPL KTGVCQLDNA NVTDAILSRA GGSIADFTGH
RQTAFRELER VLNFPQSNLC LKREKQDESC SLTQALPSEL KVSADNVSLT GAVSLASMLT
EIFLLQQAQG MPEPGWGRIT DSHQWNTLLS LHNAQFYLLQ RTPEVARSRA TPLLDLIKTA
LTPHPPQKQA YGVTLPTSVL FIAGHDTNLA NLGGALELNW TLPGQPDNTP PGGELVFERW
RRLSDNSQWI QVSLVFQTLQ QMRDKTPLSL NTPPGEVKLT LAGCEERNAQ GMCSLAGFTQ
IVNEARIPAC SL
