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P00634

- PPB_ECOLI

UniProt

P00634 - PPB_ECOLI

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Protein
Alkaline phosphatase
Gene
phoA, b0383, JW0374
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactori

Binds 1 magnesium ion.
Binds 2 zinc ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Magnesium
Metal bindingi73 – 731Zinc 2
Active sitei124 – 1241Phosphoserine intermediate
Metal bindingi175 – 1751Magnesium
Metal bindingi177 – 1771Magnesium
Metal bindingi344 – 3441Magnesium
Metal bindingi349 – 3491Zinc 1
Metal bindingi353 – 3531Zinc 1
Metal bindingi391 – 3911Zinc 2
Metal bindingi392 – 3921Zinc 2
Metal bindingi434 – 4341Zinc 1

GO - Molecular functioni

  1. alkaline phosphatase activity Source: EcoCyc
  2. hydrogenase (acceptor) activity Source: EcoCyc
  3. magnesium ion binding Source: EcoCyc
  4. oxidoreductase activity, acting on phosphorus or arsenic in donors Source: EcoliWiki
  5. protein binding Source: IntAct
  6. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. dephosphorylation Source: EcoCyc
  2. oxidation-reduction process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:ALKAPHOSPHA-MONOMER.
ECOL316407:JW0374-MONOMER.
MetaCyc:ALKAPHOSPHA-MONOMER.
SABIO-RKP00634.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline phosphatase (EC:3.1.3.1)
Short name:
APase
Gene namesi
Name:phoA
Ordered Locus Names:b0383, JW0374
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10727. phoA.

Subcellular locationi

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: EcoCyc
  2. periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121
Add
BLAST
Chaini22 – 471450Alkaline phosphatase
PRO_0000024012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi190 ↔ 200
Disulfide bondi308 ↔ 358

Keywords - PTMi

Disulfide bond, Phosphoprotein

Expressioni

Gene expression databases

GenevestigatoriP00634.

Interactioni

Subunit structurei

Isozymes 1 and 3 are a dimer of identical chains, isozyme 2 is a dimer of heterogeneous chains, one of each of the subunits from isozymes 1 and 3.

Binary interactionsi

WithEntry#Exp.IntActNotes
dsbAP0AEG42EBI-552958,EBI-549711

Protein-protein interaction databases

DIPiDIP-10496N.
IntActiP00634. 4 interactions.
MINTiMINT-1283619.
STRINGi511145.b0383.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni41 – 444
Helixi52 – 587
Beta strandi65 – 728
Helixi77 – 8711
Helixi97 – 993
Beta strandi101 – 1077
Turni113 – 1153
Beta strandi118 – 1214
Helixi124 – 13310
Beta strandi142 – 1443
Helixi154 – 1607
Beta strandi164 – 1729
Helixi176 – 1794
Turni180 – 1823
Beta strandi185 – 1873
Helixi193 – 1997
Helixi201 – 2033
Helixi205 – 2073
Helixi213 – 2208
Beta strandi223 – 2286
Helixi231 – 2344
Beta strandi235 – 2406
Turni241 – 2444
Helixi247 – 2537
Beta strandi257 – 2593
Helixi262 – 2676
Beta strandi272 – 2754
Beta strandi277 – 2804
Beta strandi282 – 2854
Beta strandi289 – 2913
Helixi299 – 3024
Helixi312 – 3143
Beta strandi316 – 3183
Helixi321 – 33212
Beta strandi339 – 3457
Helixi347 – 3537
Helixi357 – 38125
Beta strandi382 – 3898
Beta strandi391 – 3933
Beta strandi397 – 3993
Beta strandi401 – 4033
Beta strandi406 – 4138
Beta strandi417 – 4248
Beta strandi428 – 4314
Beta strandi433 – 4353
Beta strandi439 – 4457
Helixi448 – 4514
Beta strandi452 – 4565
Helixi457 – 46711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJAX-ray2.50A/B23-471[»]
1AJBX-ray2.50A/B23-471[»]
1AJCX-ray2.50A/B23-471[»]
1AJDX-ray2.50A/B23-471[»]
1ALHX-ray2.50A/B26-471[»]
1ALIX-ray2.20A/B23-471[»]
1ALJX-ray2.60A/B23-471[»]
1ALKX-ray2.00A/B23-471[»]
1ANIX-ray2.50A/B26-471[»]
1ANJX-ray2.30A/B26-471[»]
1B8JX-ray1.90A/B23-471[»]
1ED8X-ray1.75A/B23-471[»]
1ED9X-ray1.75A/B23-471[»]
1ELXX-ray2.60A/B23-471[»]
1ELYX-ray2.80A/B23-471[»]
1ELZX-ray2.80A/B23-471[»]
1EW8X-ray2.20A/B23-471[»]
1EW9X-ray2.00A/B23-471[»]
1HJKX-ray2.30A/B23-471[»]
1HQAX-ray2.25A/B23-471[»]
1KH4X-ray2.40A/B23-471[»]
1KH5X-ray2.00A/B23-471[»]
1KH7X-ray2.40A/B23-471[»]
1KH9X-ray2.50A/B23-471[»]
1KHJX-ray2.30A/B23-471[»]
1KHKX-ray2.50A/B23-471[»]
1KHLX-ray2.50A/B23-471[»]
1KHNX-ray2.60A/B23-471[»]
1URAX-ray2.04A/B26-471[»]
1URBX-ray2.14A/B26-471[»]
1Y6VX-ray1.60A/B23-471[»]
1Y7AX-ray1.77A/B23-471[»]
2ANHX-ray2.40A/B26-471[»]
2G9YX-ray2.00A/B23-471[»]
2GA3X-ray2.20A/B23-471[»]
2MLZNMR-B360-471[»]
3BDFX-ray1.40A/B22-471[»]
3BDGX-ray1.40A/B22-471[»]
3BDHX-ray1.85A/B22-471[»]
3CMRX-ray2.05A/B23-471[»]
3DPCX-ray2.30A/B23-471[»]
3DYCX-ray2.30A/B23-471[»]
3TG0X-ray1.20A/B/C/D23-471[»]
4KM4X-ray2.80A/B26-470[»]
ProteinModelPortaliP00634.
SMRiP00634. Positions 28-470.

Miscellaneous databases

EvolutionaryTraceiP00634.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1785.
HOGENOMiHOG000099117.
KOiK01077.
OMAiDKGFFLQ.
OrthoDBiEOG661H4G.
PhylomeDBiP00634.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamiPF00245. Alk_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00113. ALKPHPHTASE.
SMARTiSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00634-1 [UniParc]FASTAAdd to Basket

« Hide

MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD    50
QTAALRDSLS DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL 100
PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVDIHEKD 150
HPTILEMAKA AGLATGNVST AELQDATPAA LVAHVTSRKC YGPSATSEKC 200
PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG EWQGKTLREQ 250
AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN 300
IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK 350
QDHAANPCGQ IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA 400
PDTKAPGLTQ ALNTKDGAVM VMSYGNSEED SQEHTGSQLR IAAYGPHAAN 450
VVGLTDQTDL FYTMKAALGL K 471
Length:471
Mass (Da):49,439
Last modified:August 13, 1987 - v1
Checksum:i8A8DE1F29D9D9253
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221Missing in isozyme 3.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101L → V in AAA23431. 1 Publication
Sequence conflicti78 – 803SEI → WGS in AAA24359. 1 Publication
Sequence conflicti198 – 1981E → Q AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04586 Genomic DNA. Translation: CAA28257.1.
M13345 Genomic DNA. Translation: AAA83893.1.
M29664 Genomic DNA. Translation: AAA24364.1.
M29665 Genomic DNA. Translation: AAA24365.1.
U73857 Genomic DNA. Translation: AAB18107.1.
U00096 Genomic DNA. Translation: AAC73486.2.
AP009048 Genomic DNA. Translation: BAE76164.1.
M33536 Genomic DNA. Translation: AAA24372.1.
J01659 Genomic DNA. Translation: AAA24359.2.
J01660 Genomic DNA. Translation: AAA24360.1.
J01661 Genomic DNA. Translation: AAA24361.1.
J05005 Genomic DNA. Translation: AAA24362.1.
M14399 mRNA. Translation: AAA23431.1.
M13763 Genomic DNA. Translation: AAA24358.1.
PIRiA00776. PAECA.
RefSeqiNP_414917.2. NC_000913.3.
YP_488676.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73486; AAC73486; b0383.
BAE76164; BAE76164; BAE76164.
GeneIDi12930833.
945041.
KEGGiecj:Y75_p0372.
eco:b0383.
PATRICi32115907. VBIEscCol129921_0395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04586 Genomic DNA. Translation: CAA28257.1 .
M13345 Genomic DNA. Translation: AAA83893.1 .
M29664 Genomic DNA. Translation: AAA24364.1 .
M29665 Genomic DNA. Translation: AAA24365.1 .
U73857 Genomic DNA. Translation: AAB18107.1 .
U00096 Genomic DNA. Translation: AAC73486.2 .
AP009048 Genomic DNA. Translation: BAE76164.1 .
M33536 Genomic DNA. Translation: AAA24372.1 .
J01659 Genomic DNA. Translation: AAA24359.2 .
J01660 Genomic DNA. Translation: AAA24360.1 .
J01661 Genomic DNA. Translation: AAA24361.1 .
J05005 Genomic DNA. Translation: AAA24362.1 .
M14399 mRNA. Translation: AAA23431.1 .
M13763 Genomic DNA. Translation: AAA24358.1 .
PIRi A00776. PAECA.
RefSeqi NP_414917.2. NC_000913.3.
YP_488676.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AJA X-ray 2.50 A/B 23-471 [» ]
1AJB X-ray 2.50 A/B 23-471 [» ]
1AJC X-ray 2.50 A/B 23-471 [» ]
1AJD X-ray 2.50 A/B 23-471 [» ]
1ALH X-ray 2.50 A/B 26-471 [» ]
1ALI X-ray 2.20 A/B 23-471 [» ]
1ALJ X-ray 2.60 A/B 23-471 [» ]
1ALK X-ray 2.00 A/B 23-471 [» ]
1ANI X-ray 2.50 A/B 26-471 [» ]
1ANJ X-ray 2.30 A/B 26-471 [» ]
1B8J X-ray 1.90 A/B 23-471 [» ]
1ED8 X-ray 1.75 A/B 23-471 [» ]
1ED9 X-ray 1.75 A/B 23-471 [» ]
1ELX X-ray 2.60 A/B 23-471 [» ]
1ELY X-ray 2.80 A/B 23-471 [» ]
1ELZ X-ray 2.80 A/B 23-471 [» ]
1EW8 X-ray 2.20 A/B 23-471 [» ]
1EW9 X-ray 2.00 A/B 23-471 [» ]
1HJK X-ray 2.30 A/B 23-471 [» ]
1HQA X-ray 2.25 A/B 23-471 [» ]
1KH4 X-ray 2.40 A/B 23-471 [» ]
1KH5 X-ray 2.00 A/B 23-471 [» ]
1KH7 X-ray 2.40 A/B 23-471 [» ]
1KH9 X-ray 2.50 A/B 23-471 [» ]
1KHJ X-ray 2.30 A/B 23-471 [» ]
1KHK X-ray 2.50 A/B 23-471 [» ]
1KHL X-ray 2.50 A/B 23-471 [» ]
1KHN X-ray 2.60 A/B 23-471 [» ]
1URA X-ray 2.04 A/B 26-471 [» ]
1URB X-ray 2.14 A/B 26-471 [» ]
1Y6V X-ray 1.60 A/B 23-471 [» ]
1Y7A X-ray 1.77 A/B 23-471 [» ]
2ANH X-ray 2.40 A/B 26-471 [» ]
2G9Y X-ray 2.00 A/B 23-471 [» ]
2GA3 X-ray 2.20 A/B 23-471 [» ]
2MLZ NMR - B 360-471 [» ]
3BDF X-ray 1.40 A/B 22-471 [» ]
3BDG X-ray 1.40 A/B 22-471 [» ]
3BDH X-ray 1.85 A/B 22-471 [» ]
3CMR X-ray 2.05 A/B 23-471 [» ]
3DPC X-ray 2.30 A/B 23-471 [» ]
3DYC X-ray 2.30 A/B 23-471 [» ]
3TG0 X-ray 1.20 A/B/C/D 23-471 [» ]
4KM4 X-ray 2.80 A/B 26-470 [» ]
ProteinModelPortali P00634.
SMRi P00634. Positions 28-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10496N.
IntActi P00634. 4 interactions.
MINTi MINT-1283619.
STRINGi 511145.b0383.

Chemistry

ChEMBLi CHEMBL4217.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73486 ; AAC73486 ; b0383 .
BAE76164 ; BAE76164 ; BAE76164 .
GeneIDi 12930833.
945041.
KEGGi ecj:Y75_p0372.
eco:b0383.
PATRICi 32115907. VBIEscCol129921_0395.

Organism-specific databases

EchoBASEi EB0720.
EcoGenei EG10727. phoA.

Phylogenomic databases

eggNOGi COG1785.
HOGENOMi HOG000099117.
KOi K01077.
OMAi DKGFFLQ.
OrthoDBi EOG661H4G.
PhylomeDBi P00634.

Enzyme and pathway databases

BioCyci EcoCyc:ALKAPHOSPHA-MONOMER.
ECOL316407:JW0374-MONOMER.
MetaCyc:ALKAPHOSPHA-MONOMER.
SABIO-RK P00634.

Miscellaneous databases

EvolutionaryTracei P00634.
PROi P00634.

Gene expression databases

Genevestigatori P00634.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view ]
Pfami PF00245. Alk_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00113. ALKPHPHTASE.
SMARTi SM00098. alkPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the gene for alkaline phosphatase from Escherichia coli JM83."
    Shuttleworth H., Taylor J., Minton N.
    Nucleic Acids Res. 14:8689-8689(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / ATCC 35607 / JM83.
  2. "Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli."
    Chang C.N., Kuang W.-J., Chen E.Y.
    Gene 44:121-125(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Genetic exchange among natural isolates of bacteria: recombination within the phoA gene of Escherichia coli."
    Dubose R.F., Dykhuizen D.E., Hartl D.L.
    Proc. Natl. Acad. Sci. U.S.A. 85:7036-7040(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase."
    Agrawal D.K., Wanner B.L.
    J. Bacteriol. 172:3180-3190(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
  8. "The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli."
    Kikuchi Y., Yoda K., Yamasaki M., Tamura G.
    Nucleic Acids Res. 9:5671-5678(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
  9. Cited for: PROTEIN SEQUENCE OF 23-471 (ISOZYME 3).
  10. "Signal sequence of alkaline phosphatase of Escherichia coli."
    Inouye H., Barnes W., Beckwith J.
    J. Bacteriol. 149:434-439(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-193 AND 385-399.
  11. "Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli."
    Laforet G.A., Kaiser E.T., Kendall D.A.
    J. Biol. Chem. 264:14478-14485(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
  12. "Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable."
    Gray G.L., Baldridge J.S., McKeown K.S., Heyneker H.L., Chang C.N.
    Gene 39:247-254(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  13. "Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli."
    Michaelis S., Hunt J.F., Beckwith J.
    J. Bacteriol. 167:160-167(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  14. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  15. "Refined structure of alkaline phosphatase from Escherichia coli at 2.8-A resolution."
    Sowadski J.M., Handschumacher M.D., Krishna Murthy H.M., Foster B.A., Wyckoff H.W.
    J. Mol. Biol. 186:417-433(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  16. "Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis."
    Kim E.E., Wyckoff H.W.
    J. Mol. Biol. 218:449-464(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  17. "Crystallographic analysis of reversible metal binding observed in a mutant (Asp153-->Gly) of Escherichia coli alkaline phosphatase."
    Dealwis C.G., Brennan C., Christianson K., Mandecki W., Abad-Zapatero C.
    Biochemistry 34:13967-13973(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLY-175.
  18. "Kinetic and X-ray structural studies of a mutant Escherichia coli alkaline phosphatase (His-412-->Gln) at one of the zinc binding sites."
    Ma L., Kantrowitz E.R.
    Biochemistry 35:2394-2402(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT GLN-434.
  19. "Trapping and visualization of a covalent enzyme-phosphate intermediate."
    Murphy J.E., Stec B., Ma L., Kantrowitz E.R.
    Nat. Struct. Biol. 4:618-622(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  20. "Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102."
    Stec B., Hehir M.J., Brennan C., Nolte M., Kantrowitz E.R.
    J. Mol. Biol. 277:647-662(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  21. "A model of the transition state in the alkaline phosphatase reaction."
    Holtz K.M., Stec B., Kantrowitz E.R.
    J. Biol. Chem. 274:8351-8354(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiPPB_ECOLI
AccessioniPrimary (citable) accession number: P00634
Secondary accession number(s): P77801
, P78051, Q2MC42, Q47041
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: September 3, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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