Identification
Name:Alkaline phosphatase
Synonyms:
  • APase
Gene Name:phoA
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:A phosphate monoester + H(2)O = an alcohol + phosphate
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+3 ThumbThumb+3 Thumb
Thumb+ThumbAlcohol+Thumb
SMPDB Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
A phosphate monoester+Thumban alcohol+Thumb
A phosphate monoester + Water → an alcohol + Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB012324-NitrophenolMetaboCard
ECMDB241834-nitrophenylphosphateMetaboCard
ECMDB022757,8-DihydroneopterinMetaboCard
ECMDB00050AdenosineMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB01144Dihydroneopterin triphosphateMetaboCard
ECMDB01362Hydrogen (gas)MetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00902NADMetaboCard
ECMDB00217NADPMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB20468PhosphonateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphatase activity
phosphoric ester hydrolase activity
Process
metabolic process
Gene Properties
Blattner:b0383
Gene OrientationClockwise
Centisome Percentage:8.64
Left Sequence End400971
Right Sequence End402386
Gene Sequence:
>1416 bp
GTGAAACAAAGCACTATTGCACTGGCACTCTTACCGTTACTGTTTACCCCTGTGACAAAA
GCCCGGACACCAGAAATGCCTGTTCTGGAAAACCGGGCTGCTCAGGGCGATATTACTGCA
CCCGGCGGTGCTCGCCGTTTAACGGGTGATCAGACTGCCGCTCTGCGTGATTCTCTTAGC
GATAAACCTGCAAAAAATATTATTTTGCTGATTGGCGATGGGATGGGGGACTCGGAAATT
ACTGCCGCACGTAATTATGCCGAAGGTGCGGGCGGCTTTTTTAAAGGTATAGATGCCTTA
CCGCTTACCGGGCAATACACTCACTATGCGCTGAATAAAAAAACCGGCAAACCGGACTAC
GTCACCGACTCGGCTGCATCAGCAACCGCCTGGTCAACCGGTGTCAAAACCTATAACGGC
GCGCTGGGCGTCGATATTCACGAAAAAGATCACCCAACGATTCTGGAAATGGCAAAAGCC
GCAGGTCTGGCGACCGGTAACGTTTCTACCGCAGAGTTGCAGGATGCCACGCCCGCTGCG
CTGGTGGCACATGTGACCTCGCGCAAATGCTACGGTCCGAGCGCGACCAGTGAAAAATGT
CCGGGTAACGCTCTGGAAAAAGGCGGAAAAGGATCGATTACCGAACAGCTGCTTAACGCT
CGTGCCGACGTTACGCTTGGCGGCGGCGCAAAAACCTTTGCTGAAACGGCAACCGCTGGT
GAATGGCAGGGAAAAACGCTGCGTGAACAGGCACAGGCGCGTGGTTATCAGTTGGTGAGC
GATGCTGCCTCACTGAATTCGGTGACGGAAGCGAATCAGCAAAAACCCCTGCTTGGCCTG
TTTGCTGACGGCAATATGCCAGTGCGCTGGCTAGGACCGAAAGCAACGTACCATGGCAAT
ATCGATAAGCCCGCAGTCACCTGTACGCCAAATCCGCAACGTAATGACAGTGTACCAACC
CTGGCGCAGATGACCGACAAAGCCATTGAATTGTTGAGTAAAAATGAGAAAGGCTTTTTC
CTGCAAGTTGAAGGTGCGTCAATCGATAAACAGGATCATGCTGCGAATCCTTGTGGGCAA
ATTGGCGAGACGGTCGATCTCGATGAAGCCGTACAACGGGCGCTGGAATTCGCTAAAAAG
GAGGGTAACACGCTGGTCATAGTCACCGCTGATCACGCCCACGCCAGCCAGATTGTTGCG
CCGGATACCAAAGCTCCGGGCCTCACCCAGGCGCTAAATACCAAAGATGGCGCAGTGATG
GTGATGAGTTACGGGAACTCCGAAGAGGATTCACAAGAACATACCGGCAGTCAGTTGCGT
ATTGCGGCGTATGGCCCGCATGCCGCCAATGTTGTTGGACTGACCGACCAGACCGATCTC
TTCTACACCATGAAAGCCGCTCTGGGGCTGAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:471
Protein Molecular Weight:49438
Protein Theoretical pI:6
PDB File:1EW9
Signaling Regions:
  • 1-21
Transmembrane Regions:
  • None
Protein Sequence:
>Alkaline phosphatase
MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLS
DKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDY
VTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAA
LVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAG
EWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGN
IDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQ
IGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVM
VMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
References
External Links:
ResourceLink
Uniprot ID:P00634
Uniprot Name:PPB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674524
PDB ID:1EW9
Ecogene ID:EG10727
Ecocyc:EG10727
ColiBase:b0383
Kegg Gene:b0383
EchoBASE ID:EB0720
CCDB:PPB_ECOLI
BacMap:49176017
General Reference:
  • Agrawal, D. K., Wanner, B. L. (1990). "A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase." J Bacteriol 172:3180-3190. Pubmed: 2345142
  • 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
  • Bradshaw, R. A., Cancedda, F., Ericsson, L. H., Neumann, P. A., Piccoli, S. P., Schlesinger, M. J., Shriefer, K., Walsh, K. A. (1981). "Amino acid sequence of Escherichia coli alkaline phosphatase." Proc Natl Acad Sci U S A 78:3473-3477. Pubmed: 7022451
  • Chang, C. N., Kuang, W. J., Chen, E. Y. (1986). "Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli." Gene 44:121-125. Pubmed: 3533724
  • Dealwis, C. G., Brennan, C., Christianson, K., Mandecki, W., Abad-Zapatero, C. (1995). "Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase." Biochemistry 34:13967-13973. Pubmed: 7577993
  • DuBose, R. F., Dykhuizen, D. E., Hartl, D. L. (1988). "Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli." Proc Natl Acad Sci U S A 85:7036-7040. Pubmed: 3045828
  • Gray, G. L., Baldridge, J. S., McKeown, K. S., Heyneker, H. L., Chang, C. N. (1985). "Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable." Gene 39:247-254. Pubmed: 3912261
  • 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
  • Holtz, K. M., Stec, B., Kantrowitz, E. R. (1999). "A model of the transition state in the alkaline phosphatase reaction." J Biol Chem 274:8351-8354. Pubmed: 10085061
  • Inouye, H., Barnes, W., Beckwith, J. (1982). "Signal sequence of alkaline phosphatase of Escherichia coli." J Bacteriol 149:434-439. Pubmed: 7035431
  • Kikuchi, Y., Yoda, K., Yamasaki, M., Tamura, G. (1981). "The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli." Nucleic Acids Res 9:5671-5678. Pubmed: 6273802
  • Kim, E. E., Wyckoff, H. W. (1991). "Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis." J Mol Biol 218:449-464. Pubmed: 2010919
  • Laforet, G. A., Kaiser, E. T., Kendall, D. A. (1989). "Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli." J Biol Chem 264:14478-14485. Pubmed: 2668291
  • Ma, L., Kantrowitz, E. R. (1996). "Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites." Biochemistry 35:2394-2402. Pubmed: 8652582
  • Michaelis, S., Hunt, J. F., Beckwith, J. (1986). "Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli." J Bacteriol 167:160-167. Pubmed: 3522543
  • Murphy, J. E., Stec, B., Ma, L., Kantrowitz, E. R. (1997). "Trapping and visualization of a covalent enzyme-phosphate intermediate." Nat Struct Biol 4:618-622. Pubmed: 9253408
  • Shuttleworth, H., Taylor, J., Minton, N. (1986). "Sequence of the gene for alkaline phosphatase from Escherichia coli JM83." Nucleic Acids Res 14:8689. Pubmed: 3537962
  • Sowadski, J. M., Handschumacher, M. D., Murthy, H. M., Foster, B. A., Wyckoff, H. W. (1985). "Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution." J Mol Biol 186:417-433. Pubmed: 3910843
  • Stec, B., Hehir, M. J., Brennan, C., Nolte, M., Kantrowitz, E. R. (1998). "Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102." J Mol Biol 277:647-662. Pubmed: 9533886