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Periplasmic AppA protein [Includes: Phosphoanhydride phosphohydrolase (EC 3.1.3.2) (pH 2.5 acid phosphatase) (AP); 4-phytase (EC 3.1.3.26)]

 PPA_ECOLI               Reviewed;         432 AA.
P07102;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 2.
30-AUG-2017, entry version 152.
RecName: Full=Periplasmic AppA protein;
Includes:
RecName: Full=Phosphoanhydride phosphohydrolase;
EC=3.1.3.2;
AltName: Full=pH 2.5 acid phosphatase;
Short=AP;
Includes:
RecName: Full=4-phytase;
EC=3.1.3.26;
Flags: Precursor;
Name=appA; OrderedLocusNames=b0980, JW0963;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-29.
STRAIN=K12;
PubMed=2168385; DOI=10.1128/jb.172.9.5497-5500.1990;
Dassa J., Marck C., Boquet P.L.;
"The complete nucleotide sequence of the Escherichia coli gene appA
reveals significant homology between pH 2.5 acid phosphatase and
glucose-1-phosphatase.";
J. Bacteriol. 172:5497-5500(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112.
PubMed=3038201; DOI=10.1016/0300-9084(87)90045-9;
Touati E., Danchin A.;
"The structure of the promoter and amino terminal region of the pH 2.5
acid phosphatase structural gene (appA) of E. coli: a negative control
of transcription mediated by cyclic AMP.";
Biochimie 69:215-221(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
STRAIN=K12;
PubMed=1658595; DOI=10.1007/BF00267454;
Dassa J., Fsihi H., Marck C., Dion M., Kieffer-Bontemps M.,
Boquet P.L.;
"A new oxygen-regulated operon in Escherichia coli comprises the genes
for a putative third cytochrome oxidase and for pH 2.5 acid
phosphatase (appA).";
Mol. Gen. Genet. 229:341-352(1991).
[7]
CHARACTERIZATION, AND PROTEIN SEQUENCE OF 23-34.
Greiner R., Jany K.-D.;
"Characterization of a phytase from Escherichia coli.";
Biol. Chem. Hoppe-Seyler 372:664-665(1991).
[8]
CHARACTERIZATION, AND PROTEIN SEQUENCE OF 23-35.
PubMed=8387749; DOI=10.1006/abbi.1993.1261;
Greiner R., Konietzny U., Jany K.-D.;
"Purification and characterization of two phytases from Escherichia
coli.";
Arch. Biochem. Biophys. 303:107-113(1993).
[9]
CHARACTERIZATION.
PubMed=10696472; DOI=10.1139/cjm-46-1-59;
Golovan S., Wang G., Zhang J., Forsberg C.W.;
"Characterization and overproduction of the Escherichia coli appA
encoded bifunctional enzyme that exhibits both phytase and acid
phosphatase activities.";
Can. J. Microbiol. 46:59-71(2000).
[10]
MUTAGENESIS.
PubMed=1429631;
Ostanin K., Harms E.H., Stevis P.E., Kuciel R., Zhou M.-M.,
van Etten R.L.;
"Overexpression, site-directed mutagenesis, and mechanism of
Escherichia coli acid phosphatase.";
J. Biol. Chem. 267:22830-22836(1992).
[11]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INOSITOL
HEXAKISPHOSPHATE.
PubMed=10655611; DOI=10.1038/72371;
Lim D., Golovan S., Forsberg C.W., Jia Z.;
"Crystal structures of Escherichia coli phytase and its complex with
phytate.";
Nat. Struct. Biol. 7:108-113(2000).
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate.
-!- CATALYTIC ACTIVITY: Myo-inositol hexakisphosphate + H(2)O = 1D-
myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10655611}.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- INDUCTION: In addition to cAMP-mediated control, this enzyme is
induced when bacterial cultures reach stationary phase; its
synthesis is triggered by phosphate starvation or a shift from
aerobic to anaerobic conditions.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M58708; AAA72086.1; -; Genomic_DNA.
EMBL; U00096; AAC74065.1; -; Genomic_DNA.
EMBL; AP009048; BAA35745.1; -; Genomic_DNA.
EMBL; X05471; CAA29031.1; -; Genomic_DNA.
EMBL; S63811; AAB20286.1; -; Genomic_DNA.
PIR; B36733; B36733.
RefSeq; NP_415500.1; NC_000913.3.
RefSeq; WP_001300464.1; NZ_LN832404.1.
PDB; 1DKL; X-ray; 2.30 A; A/B=23-432.
PDB; 1DKM; X-ray; 2.25 A; A=23-432.
PDB; 1DKN; X-ray; 2.40 A; A=23-432.
PDB; 1DKO; X-ray; 2.38 A; A=23-432.
PDB; 1DKP; X-ray; 2.28 A; A=23-432.
PDB; 1DKQ; X-ray; 2.05 A; A=23-432.
PDB; 4TSR; X-ray; 2.07 A; A=23-432.
PDBsum; 1DKL; -.
PDBsum; 1DKM; -.
PDBsum; 1DKN; -.
PDBsum; 1DKO; -.
PDBsum; 1DKP; -.
PDBsum; 1DKQ; -.
PDBsum; 4TSR; -.
ProteinModelPortal; P07102; -.
SMR; P07102; -.
BioGrid; 4259354; 14.
IntAct; P07102; 3.
STRING; 316385.ECDH10B_1050; -.
SWISS-2DPAGE; P07102; -.
PaxDb; P07102; -.
PRIDE; P07102; -.
EnsemblBacteria; AAC74065; AAC74065; b0980.
EnsemblBacteria; BAA35745; BAA35745; BAA35745.
GeneID; 946206; -.
KEGG; ecj:JW0963; -.
KEGG; eco:b0980; -.
PATRIC; fig|1411691.4.peg.1293; -.
EchoBASE; EB0047; -.
EcoGene; EG10049; appA.
eggNOG; ENOG4105D6F; Bacteria.
eggNOG; ENOG410XRK8; LUCA.
HOGENOM; HOG000118851; -.
InParanoid; P07102; -.
KO; K01093; -.
PhylomeDB; P07102; -.
BioCyc; EcoCyc:APPA-MONOMER; -.
BioCyc; MetaCyc:APPA-MONOMER; -.
BRENDA; 3.1.3.26; 2026.
EvolutionaryTrace; P07102; -.
PRO; PR:P07102; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0008707; F:4-phytase activity; IEA:UniProtKB-EC.
GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052745; F:inositol phosphate phosphatase activity; IDA:EcoCyc.
GO; GO:0008252; F:nucleotidase activity; IDA:EcoCyc.
GO; GO:0050308; F:sugar-phosphatase activity; IDA:EcoCyc.
GO; GO:0071454; P:cellular response to anoxia; IDA:EcoCyc.
GO; GO:0016036; P:cellular response to phosphate starvation; IDA:EcoCyc.
GO; GO:0016311; P:dephosphorylation; IDA:EcoCyc.
GO; GO:0033518; P:myo-inositol hexakisphosphate dephosphorylation; IDA:EcoCyc.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 1.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Hydrolase; Multifunctional enzyme; Periplasm;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:2168385,
ECO:0000269|PubMed:8387749,
ECO:0000269|Ref.7}.
CHAIN 23 432 Periplasmic AppA protein.
/FTId=PRO_0000023947.
REGION 42 46 Substrate binding.
REGION 325 327 Substrate binding.
ACT_SITE 39 39 Nucleophile.
ACT_SITE 326 326 Proton donor.
BINDING 38 38 Substrate.
BINDING 114 114 Substrate.
BINDING 289 289 Substrate.
DISULFID 99 130
DISULFID 155 430
DISULFID 200 210
DISULFID 404 413
CONFLICT 51 66 MQDVTPDAWPTWPVKL -> NAGCHPRRMANLAGKT (in
Ref. 5; CAA29031). {ECO:0000305}.
CONFLICT 75 76 EL -> DV (in Ref. 5; CAA29031).
{ECO:0000305}.
CONFLICT 112 112 D -> S (in Ref. 5; CAA29031).
{ECO:0000305}.
STRAND 27 38 {ECO:0000244|PDB:1DKQ}.
HELIX 49 53 {ECO:0000244|PDB:1DKQ}.
STRAND 63 65 {ECO:0000244|PDB:4TSR}.
HELIX 71 90 {ECO:0000244|PDB:1DKQ}.
STRAND 96 98 {ECO:0000244|PDB:1DKQ}.
TURN 102 104 {ECO:0000244|PDB:1DKQ}.
STRAND 105 109 {ECO:0000244|PDB:1DKQ}.
HELIX 113 126 {ECO:0000244|PDB:1DKQ}.
HELIX 145 147 {ECO:0000244|PDB:1DKQ}.
TURN 149 153 {ECO:0000244|PDB:1DKQ}.
HELIX 159 169 {ECO:0000244|PDB:1DKQ}.
TURN 170 172 {ECO:0000244|PDB:1DKQ}.
HELIX 174 179 {ECO:0000244|PDB:1DKQ}.
HELIX 182 192 {ECO:0000244|PDB:1DKQ}.
HELIX 194 196 {ECO:0000244|PDB:1DKQ}.
HELIX 198 201 {ECO:0000244|PDB:1DKQ}.
TURN 204 207 {ECO:0000244|PDB:1DKN}.
HELIX 212 215 {ECO:0000244|PDB:1DKQ}.
STRAND 220 222 {ECO:0000244|PDB:1DKQ}.
STRAND 227 229 {ECO:0000244|PDB:1DKQ}.
HELIX 232 249 {ECO:0000244|PDB:1DKQ}.
HELIX 254 257 {ECO:0000244|PDB:1DKQ}.
HELIX 262 279 {ECO:0000244|PDB:1DKQ}.
HELIX 283 289 {ECO:0000244|PDB:1DKQ}.
HELIX 291 301 {ECO:0000244|PDB:1DKQ}.
HELIX 310 312 {ECO:0000244|PDB:1DKQ}.
STRAND 314 316 {ECO:0000244|PDB:1DKQ}.
STRAND 318 324 {ECO:0000244|PDB:1DKQ}.
HELIX 326 336 {ECO:0000244|PDB:1DKQ}.
STRAND 345 349 {ECO:0000244|PDB:1DKQ}.
STRAND 354 362 {ECO:0000244|PDB:1DKQ}.
TURN 363 366 {ECO:0000244|PDB:1DKQ}.
STRAND 367 376 {ECO:0000244|PDB:1DKQ}.
HELIX 379 383 {ECO:0000244|PDB:1DKQ}.
STRAND 390 392 {ECO:0000244|PDB:1DKQ}.
STRAND 395 399 {ECO:0000244|PDB:1DKQ}.
STRAND 405 407 {ECO:0000244|PDB:4TSR}.
HELIX 415 425 {ECO:0000244|PDB:1DKQ}.
HELIX 428 430 {ECO:0000244|PDB:1DKQ}.
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


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