Alkaline phosphatase

Details

Name
Alkaline phosphatase
Synonyms
  • 3.1.3.1
  • APase
Gene Name
phoA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019195|Alkaline phosphatase
MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLS
DKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDY
VTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAA
LVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAG
EWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGN
IDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQ
IGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVM
VMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
Number of residues
471
Molecular Weight
49438.17
Theoretical pI
6.02
GO Classification
Functions
alkaline phosphatase activity / hydrogenase (acceptor) activity / magnesium ion binding / oxidoreductase activity, acting on phosphorus or arsenic in donors / zinc ion binding
Processes
dephosphorylation / oxidation-reduction process
Components
outer membrane-bounded periplasmic space / periplasmic space
General Function
Zinc ion binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0019196|Alkaline phosphatase (phoA)
GTGAAACAAAGCACTATTGCACTGGCACTCTTACCGTTACTGTTTACCCCTGTGACAAAA
GCCCGGACACCAGAAATGCCTGTTCTGGAAAACCGGGCTGCTCAGGGCGATATTACTGCA
CCCGGCGGTGCTCGCCGTTTAACGGGTGATCAGACTGCCGCTCTGCGTGATTCTCTTAGC
GATAAACCTGCAAAAAATATTATTTTGCTGATTGGCGATGGGATGGGGGACTCGGAAATT
ACTGCCGCACGTAATTATGCCGAAGGTGCGGGCGGCTTTTTTAAAGGTATAGATGCCTTA
CCGCTTACCGGGCAATACACTCACTATGCGCTGAATAAAAAAACCGGCAAACCGGACTAC
GTCACCGACTCGGCTGCATCAGCAACCGCCTGGTCAACCGGTGTCAAAACCTATAACGGC
GCGCTGGGCGTCGATATTCACGAAAAAGATCACCCAACGATTCTGGAAATGGCAAAAGCC
GCAGGTCTGGCGACCGGTAACGTTTCTACCGCAGAGTTGCAGGATGCCACGCCCGCTGCG
CTGGTGGCACATGTGACCTCGCGCAAATGCTACGGTCCGAGCGCGACCAGTGAAAAATGT
CCGGGTAACGCTCTGGAAAAAGGCGGAAAAGGATCGATTACCGAACAGCTGCTTAACGCT
CGTGCCGACGTTACGCTTGGCGGCGGCGCAAAAACCTTTGCTGAAACGGCAACCGCTGGT
GAATGGCAGGGAAAAACGCTGCGTGAACAGGCACAGGCGCGTGGTTATCAGTTGGTGAGC
GATGCTGCCTCACTGAATTCGGTGACGGAAGCGAATCAGCAAAAACCCCTGCTTGGCCTG
TTTGCTGACGGCAATATGCCAGTGCGCTGGCTAGGACCGAAAGCAACGTACCATGGCAAT
ATCGATAAGCCCGCAGTCACCTGTACGCCAAATCCGCAACGTAATGACAGTGTACCAACC
CTGGCGCAGATGACCGACAAAGCCATTGAATTGTTGAGTAAAAATGAGAAAGGCTTTTTC
CTGCAAGTTGAAGGTGCGTCAATCGATAAACAGGATCATGCTGCGAATCCTTGTGGGCAA
ATTGGCGAGACGGTCGATCTCGATGAAGCCGTACAACGGGCGCTGGAATTCGCTAAAAAG
GAGGGTAACACGCTGGTCATAGTCACCGCTGATCACGCCCACGCCAGCCAGATTGTTGCG
CCGGATACCAAAGCTCCGGGCCTCACCCAGGCGCTAAATACCAAAGATGGCGCAGTGATG
GTGATGAGTTACGGGAACTCCGAAGAGGATTCACAAGAACATACCGGCAGTCAGTTGCGT
ATTGCGGCGTATGGCCCGCATGCCGCCAATGTTGTTGGACTGACCGACCAGACCGATCTC
TTCTACACCATGAAAGCCGCTCTGGGGCTGAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00634
UniProtKB Entry NamePPB_ECOLI
GenBank Protein ID581187
GenBank Gene IDX04586
General References
  1. Shuttleworth H, Taylor J, Minton N: Sequence of the gene for alkaline phosphatase from Escherichia coli JM83. Nucleic Acids Res. 1986 Nov 11;14(21):8689. [Article]
  2. Chang CN, Kuang WJ, Chen EY: Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene. 1986;44(1):121-5. [Article]
  3. DuBose RF, Dykhuizen DE, Hartl DL: Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli. Proc Natl Acad Sci U S A. 1988 Sep;85(18):7036-40. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Agrawal DK, Wanner BL: A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase. J Bacteriol. 1990 Jun;172(6):3180-90. [Article]
  7. Kikuchi Y, Yoda K, Yamasaki M, Tamura G: The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli. Nucleic Acids Res. 1981 Nov 11;9(21):5671-8. [Article]
  8. Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA: Amino acid sequence of Escherichia coli alkaline phosphatase. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3473-7. [Article]
  9. Inouye H, Barnes W, Beckwith J: Signal sequence of alkaline phosphatase of Escherichia coli. J Bacteriol. 1982 Feb;149(2):434-9. [Article]
  10. Laforet GA, Kaiser ET, Kendall DA: Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli. J Biol Chem. 1989 Aug 25;264(24):14478-85. [Article]
  11. Gray GL, Baldridge JS, McKeown KS, Heyneker HL, Chang CN: Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable. Gene. 1985;39(2-3):247-54. [Article]
  12. Michaelis S, Hunt JF, Beckwith J: Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli. J Bacteriol. 1986 Jul;167(1):160-7. [Article]
  13. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  14. Sowadski JM, Handschumacher MD, Murthy HM, Foster BA, Wyckoff HW: Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution. J Mol Biol. 1985 Nov 20;186(2):417-33. [Article]
  15. Kim EE, Wyckoff HW: Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J Mol Biol. 1991 Mar 20;218(2):449-64. [Article]
  16. Dealwis CG, Brennan C, Christianson K, Mandecki W, Abad-Zapatero C: Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase. Biochemistry. 1995 Oct 31;34(43):13967-73. [Article]
  17. Ma L, Kantrowitz ER: Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites. Biochemistry. 1996 Feb 20;35(7):2394-402. [Article]
  18. Murphy JE, Stec B, Ma L, Kantrowitz ER: Trapping and visualization of a covalent enzyme-phosphate intermediate. Nat Struct Biol. 1997 Aug;4(8):618-22. [Article]
  19. Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER: 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. 1998 Apr 3;277(3):647-62. [Article]
  20. Holtz KM, Stec B, Kantrowitz ER: A model of the transition state in the alkaline phosphatase reaction. J Biol Chem. 1999 Mar 26;274(13):8351-4. [Article]
  21. Saio T, Guan X, Rossi P, Economou A, Kalodimos CG: Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science. 2014 May 9;344(6184):1250494. doi: 10.1126/science.1250494. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02823Phosphonoacetic AcidexperimentalunknownDetails
DB03498Mercaptomethyl PhosphonateexperimentalunknownDetails
DB04031Serine vanadateexperimentalunknownDetails
DB04522DexfosfoserineexperimentalunknownDetails