Periplasmic AppA protein (P07102)

Identification
Name:Periplasmic AppA protein
Synonyms:
  • Phosphoanhydride phosphohydrolase
  • pH 2.5 acid phosphatase
  • AP
  • 4-phytase
Gene Name:appA
Enzyme Class:
Biological Properties
General Function:Involved in acid phosphatase activity
Specific Function:A phosphate monoester + H(2)O = an alcohol + phosphate
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
  • 1,4-Dichlorobenzene degradation ec00627
  • Inositol phosphate metabolism ec00562
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Flavin Mononucleotide + 1.0Water ↔ 1.0Riboflavin + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Myo-inositol hexakisphosphate + 1.0Water ↔ 1.01-Myo-inositol 1,2,3,4,5-pentakisphosphate + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Alcohol+1.0Thumb
1.0Orthophosphoric monoester + 1.0Water ↔ 1.0Alcohol + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Myo-inositol hexakisphosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Myo-inositol hexakisphosphate + 1.0Water + 1.0Myo-inositol hexakisphosphate → 1.01-Myo-inositol 1,2,3,4,5-pentakisphosphate + 1.0Phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Guanosine triphosphate + 1.0Water → 1.0Guanosine diphosphate + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Flavin Mononucleotide + 1.0Water ↔ 1.0Riboflavin + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Myo-inositol hexakisphosphate + 1.0Water ↔ 1.01-Myo-inositol 1,2,3,4,5-pentakisphosphate + 1.0Phosphate
ReactionCard
Complex Reactions:
6.0Thumb+1.0Thumb → 1.0Thumb+6.0Thumb
6.0Water + 1.0Myo-inositol hexakisphosphate → 1.0Inositol + 6.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB041081-Myo-inositol 1,2,3,4,5-pentakisphosphateMetaboCard
ECMDB012324-NitrophenolMetaboCard
ECMDB241834-nitrophenylphosphateMetaboCard
ECMDB01520Flavin MononucleotideMetaboCard
ECMDB01201Guanosine diphosphateMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00160InositolMetaboCard
ECMDB20161Inositol 1,2,3,5,6-pentakisphosphateMetaboCard
ECMDB00158L-TyrosineMetaboCard
ECMDB03502Myo-inositol hexakisphosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB21276PhosphotyrosineMetaboCard
ECMDB00244RiboflavinMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
acid phosphatase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphatase activity
phosphoric ester hydrolase activity
Gene Properties
Blattner:b0980
Gene OrientationClockwise
Centisome Percentage:22.41
Left Sequence End1039840
Right Sequence End1041138
Gene Sequence:
>1299 bp
ATGACACTCACGCTCAATAGACAACTTCTCACCTCACGCCAGATTCTGGTGGCCTTTAGC
GGCGGGCTTGACTCCACCGTTCTGCTGCATCAGTTGGTGCAGTGGCGGACGGAAAATCCG
GGTGTCGCTCTGCGCGCTATTCATGTGCATCACGGTTTAAGTGCCAATGCCGATGCCTGG
GTTACGCATTGCGAAAACGTCTGCCAACAGTGGCAGGTGCCGCTGGTGGTCGAACGCGTA
CAACTTGCGCAAGAAGGACTGGGCATTGAGGCCCAGGCGCGGCAGGCACGTTATCAGGCA
TTTGCCCGCACCTTGTTGCCCGGTGAAGTGCTGGTCACCGCGCAACATCTCGACGATCAA
TGTGAAACCTTTCTGCTGGCGCTAAAACGCGGCAGTGGCCCTGCCGGGCTTTCGGCTATG
GCGGAAGTCTCGGAGTTTGCCGGAACGCGGCTTATTCGCCCGTTGCTCGCCCGCACGCGG
GGGGAACTGGTGCAGTGGGCGCGTCAGTATGATTTACGCTGGATTGAAGACGAAAGTAAT
CAGGACGACTCATACGATCGTAACTTTCTGCGCCTGCGCGTAGTGCCGTTATTGCAGCAG
CGTTGGCCGCATTTTGCCGAAGCAACGGCCCGCAGCGCCGCACTTTGTGCTGAACAAGAG
AGCCTGCTGGATGAACTGCTGGCAGATGATTTAGCACACTGTCAATCGCCGCAGGGGACG
CTGCAGATTGTGCCAATGCTGGCGATGAGTGATGCCCGCCGCGCGGCGATTATCCGCCGC
TGGCTGGCAGGGCAGAATGCACCGATGCCTTCCCGCGACGCGTTGGTGAGGATCTGGCAG
GAAGTGGCGCTGGCGCGGGAAGATGCCTCACCCTGTTTACGTTTGGGCGCGTTTGAAATC
CGACGCTATCAGTCGCAACTGTGGTGGATTAAATCCGTCACCGGGCAAAGCGAAAACATT
GTGCCGTGGCAGACGTGGCTTCAACCGCTGGAATTACCGGCGGGGCTGGGAAGTGTACAG
CTTAATGCGGGAGGCGATATTCGCCCTCCGCGTGCAGACGAAGCGGTCAGCGTGCGTTTC
AAAGCGCCAGGATTGCTGCATATTGTCGGGCGTAACGGCGGACGTAAGCTAAAGAAAATC
TGGCAAGAGCTGGGCGTGCCGCCGTGGCTACGTGACACCACGCCACTGCTGTTTTATGGC
GAAACGCTGATTGCGGCGGCAGGGGTATTTGTGACGCAAGAAGGTGTGGCTGAAGGTGAG
AATGGCGTAAGTTTTGTCTGGCAGAAAACGCTTAGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:432
Protein Molecular Weight:47056
Protein Theoretical pI:7
PDB File:1DKL
Signaling Regions:
  • 1-22
Transmembrane Regions:
  • None
Protein Sequence:
>Periplasmic AppA protein
MKAILIPFLSLLIPLTPQSAFAQSEPELKLESVVIVSRHGVRAPTKATQLMQDVTPDAWP
TWPVKLGWLTPRGGELIAYLGHYQRQRLVADGLLAKKGCPQSGQVAIIADVDERTRKTGE
AFAAGLAPDCAITVHTQADTSSPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADFTGH
RQTAFRELERVLNFPQSNLCLKREKQDESCSLTQALPSELKVSADNVSLTGAVSLASMLT
EIFLLQQAQGMPEPGWGRITDSHQWNTLLSLHNAQFYLLQRTPEVARSRATPLLDLIKTA
LTPHPPQKQAYGVTLPTSVLFIAGHDTNLANLGGALELNWTLPGQPDNTPPGGELVFERW
RRLSDNSQWIQVSLVFQTLQQMRDKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLAGFTQ
IVNEARIPACSL
References
External Links:
ResourceLink
Uniprot ID:P07102
Uniprot Name:PPA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902929
PDB ID:1DKL
Ecogene ID:EG10049
Ecocyc:EG10049
ColiBase:b0980
Kegg Gene:b0980
EchoBASE ID:EB0047
CCDB:PPA_ECOLI
BacMap:16128946
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Dassa, J., Fsihi, H., Marck, C., Dion, M., Kieffer-Bontemps, M., Boquet, P. L. (1991). "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. Pubmed: 1658595
  • Dassa, J., Marck, C., Boquet, P. L. (1990). "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. Pubmed: 2168385
  • Golovan, S., Wang, G., Zhang, J., Forsberg, C. W. (2000). "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. Pubmed: 10696472
  • Greiner, R., Konietzny, U., Jany, K. D. (1993). "Purification and characterization of two phytases from Escherichia coli." Arch Biochem Biophys 303:107-113. Pubmed: 8387749
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Lim, D., Golovan, S., Forsberg, C. W., Jia, Z. (2000). "Crystal structures of Escherichia coli phytase and its complex with phytate." Nat Struct Biol 7:108-113. Pubmed: 10655611
  • 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., Horiuchi, T., et, a. l. .. (1996). "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. Pubmed: 8905232
  • Ostanin, K., Harms, E. H., Stevis, P. E., Kuciel, R., Zhou, M. M., Van Etten, R. L. (1992). "Overexpression, site-directed mutagenesis, and mechanism of Escherichia coli acid phosphatase." J Biol Chem 267:22830-22836. Pubmed: 1429631
  • Touati, E., Danchin, A. (1987). "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. Pubmed: 3038201