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Escherichia coli K-12 substr. MG1655 Enzyme: alkaline phosphatase



Gene: phoA Accession Numbers: EG10727 (EcoCyc), b0383, ECK0378

Synonyms: psiA

Regulation Summary Diagram: ?

Subunit composition of alkaline phosphatase = [PhoA]2

Summary:
Alkaline phosphatase is a periplasmic, homodimeric enzyme that catalyses the hydrolysis and transphosphorylation of a wide variety of phosphate monoesters [Torriani60, Heppel62, Malamy61, Chang80a]. The reaction proceeds through a phosphoseryl intermediate with the subsequent release of inorganic phosphate and alcohol [Schwartz61, Holtz99, Stec98, Stec00]. The transphosphorylation reaction results in the transfer of a phosphoryl group to the alcohol of acceptors such as Tris or ethanolamine [Dayan64, Wilson64a] . Alkaline phosphatase is a metalloenzyme, binding two zinc atoms and one magnesium ion per monomer [Plocke62a, Plocke62, Sowadski85, Janeway93].

The amount of alkaline phosphatase is optimal when cells are starved for phosphate - which is the most common environment for E.coli in the human gut - and is much reduced when there is an excess of phosphate [Torriani60]. Under conditions of limiting phosphate, alkaline phosphatase accounts for approximately 6% of the total protein synthesized [Garen60]

Alkaline phosphatase occurs in three major forms designated isozymes 1, 2 and 3 whose relative proprotions are dependent on the growth conditions [Kelley73, Schlesinger68]. The isozymes are differentiated by the presence or absence of an NH2-terminal arginine residue: present in both subunits of isozyme 1, absent in both subunits of isozyme 3 and heterogenous in isozyme 2 [Nakata78, Bradshaw81]. Removal of the N-terminal arginine is catalysed by the membrane-associated, proteolytic enyzyme Iap [Nakata77, Nakata84].

The precursor polypeptide is secreted across the inner membrane to the periplasmic space concommitant with removal of the signal sequence [Chang86a]. Folding of PhoA in vivo is catalysed by the periplasmic protein, DsbA and is thought to occur as the polypeptide elongates from the ribosome [Kadokura09].

phoA is part of the phosphate regulon; its expression is positively regulated by the PhoB transcriptional regulator [Makino86]

A single report has also suggested that the PhoA protein oxidizes phosphite to phosphate, producing molecular H2 [Yang04b].

Reviews: [Coleman92a, Holtz99, Stigbrand82, Torriani90].

Citations: [Horiuchi59, Nesmeyanova81, Applebury70, Ma95, Ma96b, Le02a, Michaelis83, Inouye77, Torriani68, Schlesinger68a]

Gene Citations: [Kikuchi81, Wanner81, Yamada89]

Locations: periplasmic space

Map Position: [400,971 -> 402,386] (8.64 centisomes)
Length: 1416 bp / 471 aa

Molecular Weight of Polypeptide: 49.439 kD (from nucleotide sequence)

pI: 6.09

Unification Links: ASAP:ABE-0001328 , CGSC:398 , DIP:DIP-10496N , EchoBASE:EB0720 , EcoGene:EG10727 , EcoliWiki:b0383 , Mint:MINT-1283619 , ModBase:P00634 , OU-Microarray:b0383 , PortEco:phoA , PR:PRO_000023540 , Protein Model Portal:P00634 , RefSeq:NP_414917 , RegulonDB:EG10727 , SMR:P00634 , String:511145.b0383 , UniProt:P00634

Relationship Links: InterPro:IN-FAMILY:IPR001952 , InterPro:IN-FAMILY:IPR017849 , InterPro:IN-FAMILY:IPR017850 , InterPro:IN-FAMILY:IPR018299 , PDB:Structure:1AJA , PDB:Structure:1AJB , PDB:Structure:1AJC , PDB:Structure:1AJD , PDB:Structure:1ALH , PDB:Structure:1ALI , PDB:Structure:1ALJ , PDB:Structure:1ALK , PDB:Structure:1ANI , PDB:Structure:1ANJ , PDB:Structure:1B8J , PDB:Structure:1ED8 , PDB:Structure:1ED9 , PDB:Structure:1ELX , PDB:Structure:1ELY , PDB:Structure:1ELZ , PDB:Structure:1EW8 , PDB:Structure:1EW9 , PDB:Structure:1HJK , PDB:Structure:1HQA , PDB:Structure:1KH4 , PDB:Structure:1KH5 , PDB:Structure:1KH7 , PDB:Structure:1KH9 , PDB:Structure:1KHJ , PDB:Structure:1KHK , PDB:Structure:1KHL , PDB:Structure:1KHN , PDB:Structure:1URA , PDB:Structure:1URB , PDB:Structure:1Y6V , PDB:Structure:1Y7A , PDB:Structure:2ANH , PDB:Structure:2G9Y , PDB:Structure:2GA3 , PDB:Structure:3BDF , PDB:Structure:3BDG , PDB:Structure:3BDH , PDB:Structure:3CMR , PDB:Structure:3DPC , PDB:Structure:3DYC , PDB:Structure:3TG0 , PDB:Structure:4KM4 , Pfam:IN-FAMILY:PF00245 , Prints:IN-FAMILY:PR00113 , Prosite:IN-FAMILY:PS00123 , Smart:IN-FAMILY:SM00098

In Paralogous Gene Group: 116 (4 members)

Gene-Reaction Schematic: ?

Instance reactions of [D-glucopyranose 6-phosphate[periplasmic space] + H2O[periplasmic space] → D-glucopyranose[periplasmic space] + phosphate[periplasmic space]] (3.1.3.58):
i1: α-D-glucose 6-phosphate + H2O → α-D-glucose + phosphate (3.1.3.58)

i2: β-D-glucose 6-phosphate + H2O → β-D-glucose + phosphate (3.1.3.58)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0016311 - dephosphorylation Inferred from experiment [Garen60]
GO:0055114 - oxidation-reduction process Inferred from experiment [Yang04b]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment [Sowadski85]
GO:0004035 - alkaline phosphatase activity Inferred from experiment Inferred by computational analysis [GOA01a, Garen60]
GO:0005515 - protein binding Inferred from experiment [Kadokura09]
GO:0008270 - zinc ion binding Inferred from experiment [Plocke62, Sowadski85]
GO:0030613 - oxidoreductase activity, acting on phosphorus or arsenic in donors Inferred from experiment [Yang04b]
GO:0033748 - hydrogenase (acceptor) activity Inferred from experiment [Yang04b]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016791 - phosphatase activity Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [DiazMejia09, Malamy64]
GO:0042597 - periplasmic space Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Malamy64]

MultiFun Terms: metabolism metabolism of other compounds phosphorous metabolism

Essentiality data for phoA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 18-Dec-2011 by Mackie A , Macquarie University


Enzymatic reaction of: alkaline phosphatase

Synonyms: APase, AP, alkaline phosphomonesterase, glycerophosphatase, orthophosphoric-monoester phosphohydrolase (alkaline optimum)

EC Number: 3.1.3.1

a phosphate monoester[periplasmic space] + H2O[periplasmic space] <=> an alcohol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for a phosphate monoester: ATP [Heppel62 ] , dATP [Heppel62 ] , UDP [Heppel62 ] , dGTP [Heppel62 ] , dTTP [Heppel62 ] , dCTP [Heppel62 ]

Cofactors or Prosthetic Groups: Mg2+ [Sowadski85], Zn2+ [Sowadski85]

Inhibitors (Competitive): phosphate [Kim91a] , arsenate [Sowadski85] , thioglycolate [Malamy64a] , vanadate [Stankiewicz88] , chromate [Stankiewicz88] , molybdate [Stankiewicz88]

Inhibitors (Unknown Mechanism): L-cysteine [Malamy64a]

pH(opt): 8.0 [Garen60]


Enzymatic reaction of: β-D-glucose 6-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.58

β-D-glucose 6-phosphate + H2O <=> β-D-glucose + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from MetaCyc 04-Feb-2014 by Caspi R , SRI International


Enzymatic reaction of: α-D-glucose 6-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.58

α-D-glucose 6-phosphate + H2O <=> α-D-glucose + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from MetaCyc 04-Feb-2014 by Caspi R , SRI International


Enzymatic reaction of: diphosphate phosphatase (alkaline phosphatase)

EC Number: 3.6.1.1

diphosphate[periplasmic space] + H2O[periplasmic space] <=> 2 phosphate[periplasmic space] + H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: triphosphate phosphatase (alkaline phosphatase)

EC Number: 3.6.1.25

PPPi[periplasmic space] + H2O[periplasmic space] <=> phosphate[periplasmic space] + diphosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: 3-phospho-L-serine phosphatase (alkaline phosphatase)

EC Number: 3.1.3.3

3-phospho-L-serine[periplasmic space] + H2O[periplasmic space] <=> L-serine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: L-threonine O-3-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

L-threonine 3-O-phosphate[periplasmic space] + H2O[periplasmic space] <=> L-threonine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: ribose 5-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

D-ribose 5-phosphate[periplasmic space] + H2O[periplasmic space] <=> aldehydo-D-ribose[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: glucose-1-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.10

α-D-glucose 1-phosphate[periplasmic space] + H2O[periplasmic space] <=> D-glucopyranose[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: glucose-6-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.58

D-glucopyranose 6-phosphate[periplasmic space] + H2O[periplasmic space] <=> D-glucopyranose[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: glycerol-2-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.19

glycerol 2-phosphate[periplasmic space] + H2O[periplasmic space] <=> glycerol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.


Enzymatic reaction of: phosphoglycerate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.20

2-phospho-D-glycerate[periplasmic space] + H2O[periplasmic space] <=> D-glycerate[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: fructose-1,6-biphosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.11

fructose 1,6-bisphosphate[periplasmic space] + H2O[periplasmic space] <=> β-D-fructofuranose 6-phosphate[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of hexitol degradation (bacteria) , glycolysis II (from fructose-6P)


Enzymatic reaction of: NADP+ phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

NADP+[periplasmic space] + H2O[periplasmic space] <=> NAD+[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: FMN phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

FMN[periplasmic space] + H2O[periplasmic space] <=> riboflavin[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: L-histidinol-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.15

L-histidinol-phosphate[periplasmic space] + H2O[periplasmic space] <=> histidinol[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: phosphoenolpyruvate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.60

phosphoenolpyruvate[periplasmic space] + H2O[periplasmic space] <=> pyruvate[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: AMP phosphatase (alkaline phosphatase)

AMP + H2O <=> adenosine + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: adenosine nucleotides degradation II


Enzymatic reaction of: dAMP phosphatase (alkaline phosphatase)

dAMP[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyadenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: 3'AMP phosphatase (alkaline phosphatase)

adenosine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> adenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: 2'AMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

adenosine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> adenosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: dGMP phosphatase (alkaline phosphatase)

dGMP[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxyguanosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: 2'GMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

guanosine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> guanosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: 2'CMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

cytidine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> cytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: 3'CMP phosphatase (alkaline phosphatase)

cytidine-3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> cytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: CMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.91

CMP + H2O <=> cytidine + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: dCMP phosphatase (alkaline phosphatase)

dCMP[periplasmic space] + H2O[periplasmic space] <=> 2'-deoxycytidine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: 2'UMP phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

uridine 2'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> uridine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: 3'UMP phosphatase (alkaline phosphatase)

uridine 3'-monophosphate[periplasmic space] + H2O[periplasmic space] <=> uridine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: UMP phosphatase (alkaline phosphatase)

UMP + H2O <=> uridine + phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: IMP phosphatase (alkaline phosphatase)

IMP[periplasmic space] + H2O[periplasmic space] <=> inosine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: pyridoxine-5'-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.74

pyridoxine 5'-phosphate[periplasmic space] + H2O[periplasmic space] <=> pyridoxine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: pyridoxal 5'-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.74

pyridoxal 5'-phosphate[periplasmic space] + H2O[periplasmic space] <=> pyridoxal[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: 4-nitrophenyl phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.41

4-nitrophenyl phosphate[periplasmic space] + H2O[periplasmic space] <=> 4-nitrophenol[periplasmic space] + phosphate[periplasmic space] + H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

Note: The enzyme may catalyze this reaction in vitro, but this reaction is not considered to be physiologically relevant.


Enzymatic reaction of: cysteamine S-phosphate phosphatase (alkaline phosphatase)

EC Number: 3.1.3.-

cysteamine S-phosphate[periplasmic space] + H2O[periplasmic space] <=> cysteamine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.


Enzymatic reaction of: phosphocholine phosphatase (alkaline phosphatase)

EC Number: 3.1.3.75

phosphocholine[periplasmic space] + H2O[periplasmic space] <=> choline[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Enzymatic reaction of: phosphoryl-ethanolamine phosphatase (alkaline phosphatase)

EC Number: 3.1.3.75

phosphoryl-ethanolamine[periplasmic space] + H2O[periplasmic space] <=> ethanolamine[periplasmic space] + phosphate[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 21
[UniProt10]
Sequence-Conflict 10
[Gray85, UniProt11]
Alternate sequence: L → V; UniProt: (in Ref. 12; AAA23431).
Extrinsic-Sequence-Variant 22
[UniProt10]
Alternate sequence: R → missing; UniProt: (in isozyme 3);
Chain 22 -> 471
[UniProt09]
UniProt: Alkaline phosphatase;
Metal-Binding-Site 73
[UniProt10]
UniProt: Magnesium;
Sequence-Conflict 78 -> 80
[Kikuchi81, UniProt10]
Alternate sequence: SEI → WGS; UniProt: (in Ref. 8; AAA24359);
Active-Site 124
[UniProt10]
UniProt: Phosphoserine intermediate;
Metal-Binding-Site 175
[UniProt10]
UniProt: Magnesium;
Metal-Binding-Site 177
[UniProt10]
UniProt: Magnesium;
Disulfide-Bond-Site 200, 190
[UniProt10]
Sequence-Conflict 198
[Bradshaw81, UniProt10]
Alternate sequence: E → Q; UniProt: (in Ref. 9; AA sequence);
Disulfide-Bond-Site 358, 308
[UniProt10]
Metal-Binding-Site 344
[UniProt10]
UniProt: Magnesium;
Metal-Binding-Site 349
[UniProt10]
UniProt: Zinc 1;
Metal-Binding-Site 353
[UniProt10]
UniProt: Zinc 1;
Metal-Binding-Site 391
[UniProt10]
UniProt: Zinc 2;
Metal-Binding-Site 392
[UniProt10]
UniProt: Zinc 2;
Metal-Binding-Site 434
[UniProt10]
UniProt: Zinc 1;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b0383 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10727; confirmed by SwissProt match.


References

Applebury70: Applebury ML, Johnson BP, Coleman JE (1970). "Phosphate binding to alkaline phosphatase. Metal ion dependence." J Biol Chem 245(19);4968-76. PMID: 4319108

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bradshaw81: Bradshaw RA, Cancedda F, Ericsson LH, Neumann PA, Piccoli SP, Schlesinger MJ, Shriefer K, Walsh KA (1981). "Amino acid sequence of Escherichia coli alkaline phosphatase." Proc Natl Acad Sci U S A 1981;78(6);3473-7. PMID: 7022451

Chang80a: Chang CN, Inouye H, Model P, Beckwith J (1980). "Processing of alkaline phosphatase precursor to the mature enzyme by an Escherichia coli inner membrane preparation." J Bacteriol 142(2);726-8. PMID: 6991486

Chang86a: Chang CN, Kuang WJ, Chen EY (1986). "Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli." Gene 1986;44(1);121-5. PMID: 3533724

Coleman92a: Coleman JE (1992). "Structure and mechanism of alkaline phosphatase." Annu Rev Biophys Biomol Struct 1992;21;441-83. PMID: 1525473

Dayan64: Dayan J, Wilson IB (1964). "The phosphorylation of Tris by alkaline phosphatase." Biochim Biophys Acta 81;620-3. PMID: 14171894

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

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Other References Related to Gene Regulation

Marzan13: Marzan LW, Hasan CM, Shimizu K (2013). "Effect of acidic condition on the metabolic regulation of Escherichia coli and its phoB mutant." Arch Microbiol 195(3);161-71. PMID: 23274360

Shuttleworth86: Shuttleworth H, Taylor J, Minton N (1986). "Sequence of the gene for alkaline phosphatase from Escherichia coli JM83." Nucleic Acids Res 14(21);8689. PMID: 3537962


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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