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Protein

Alkaline phosphatase

Gene

phoA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+Note: Binds 1 Mg2+ ion.
  • Zn2+Note: Binds 2 Zn2+ 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

  • alkaline phosphatase activity Source: EcoCyc
  • hydrogenase (acceptor) activity Source: EcoCyc
  • magnesium ion binding Source: EcoCyc
  • oxidoreductase activity, acting on phosphorus or arsenic in donors Source: EcoliWiki
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • dephosphorylation Source: EcoCyc
  • 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.
BRENDAi3.1.3.1. 2026.
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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10727. phoA.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 471450Alkaline phosphatasePRO_0000024012Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Phosphoprotein

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
LRRK2Q5S0072EBI-552958,EBI-5323863From a different organism.

Protein-protein interaction databases

DIPiDIP-10496N.
IntActiP00634. 5 interactions.
MINTiMINT-1283619.
STRINGi511145.b0383.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni41 – 444Combined sources
Helixi52 – 587Combined sources
Beta strandi65 – 728Combined sources
Helixi77 – 8711Combined sources
Helixi97 – 993Combined sources
Beta strandi101 – 1077Combined sources
Turni113 – 1153Combined sources
Beta strandi118 – 1214Combined sources
Helixi124 – 13310Combined sources
Beta strandi142 – 1443Combined sources
Helixi154 – 1607Combined sources
Beta strandi164 – 1729Combined sources
Helixi176 – 1794Combined sources
Turni180 – 1823Combined sources
Beta strandi185 – 1873Combined sources
Helixi193 – 1997Combined sources
Helixi201 – 2033Combined sources
Helixi205 – 2073Combined sources
Helixi213 – 2208Combined sources
Beta strandi223 – 2286Combined sources
Helixi231 – 2344Combined sources
Beta strandi235 – 2406Combined sources
Turni241 – 2444Combined sources
Helixi247 – 2537Combined sources
Beta strandi257 – 2593Combined sources
Helixi262 – 2676Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi289 – 2913Combined sources
Helixi299 – 3024Combined sources
Helixi312 – 3143Combined sources
Beta strandi316 – 3183Combined sources
Helixi321 – 33212Combined sources
Beta strandi339 – 3457Combined sources
Helixi347 – 3537Combined sources
Helixi357 – 38125Combined sources
Beta strandi382 – 3898Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi397 – 3993Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi406 – 4138Combined sources
Beta strandi417 – 4248Combined sources
Beta strandi428 – 4314Combined sources
Beta strandi433 – 4353Combined sources
Beta strandi439 – 4457Combined sources
Helixi448 – 4514Combined sources
Beta strandi452 – 4565Combined sources
Helixi457 – 46711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MLXNMR-B220-310[»]
2MLYNMR-B1-150[»]
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[»]
4YR1X-ray2.24A/B31-471[»]
ProteinModelPortaliP00634.
SMRiP00634. Positions 28-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00634.

Family & Domainsi

Sequence similaritiesi

Belongs to the alkaline phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1785.
HOGENOMiHOG000099117.
InParanoidiP00634.
KOiK01077.
OMAiEEGSQEH.
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

        10         20         30         40         50
MKQSTIALAL LPLLFTPVTK ARTPEMPVLE NRAAQGDITA PGGARRLTGD
60 70 80 90 100
QTAALRDSLS DKPAKNIILL IGDGMGDSEI TAARNYAEGA GGFFKGIDAL
110 120 130 140 150
PLTGQYTHYA LNKKTGKPDY VTDSAASATA WSTGVKTYNG ALGVDIHEKD
160 170 180 190 200
HPTILEMAKA AGLATGNVST AELQDATPAA LVAHVTSRKC YGPSATSEKC
210 220 230 240 250
PGNALEKGGK GSITEQLLNA RADVTLGGGA KTFAETATAG EWQGKTLREQ
260 270 280 290 300
AQARGYQLVS DAASLNSVTE ANQQKPLLGL FADGNMPVRW LGPKATYHGN
310 320 330 340 350
IDKPAVTCTP NPQRNDSVPT LAQMTDKAIE LLSKNEKGFF LQVEGASIDK
360 370 380 390 400
QDHAANPCGQ IGETVDLDEA VQRALEFAKK EGNTLVIVTA DHAHASQIVA
410 420 430 440 450
PDTKAPGLTQ ALNTKDGAVM VMSYGNSEED SQEHTGSQLR IAAYGPHAAN
460 470
VVGLTDQTDL FYTMKAALGL K
Length:471
Mass (Da):49,439
Last modified:August 13, 1987 - v1
Checksum:i8A8DE1F29D9D9253
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101L → V in AAA23431 (PubMed:3912261).Curated
Sequence conflicti78 – 803SEI → WGS in AAA24359 (PubMed:6273802).Curated
Sequence conflicti198 – 1981E → Q AA sequence (PubMed:7022451).Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000814403.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC73486; AAC73486; b0383.
BAE76164; BAE76164; BAE76164.
GeneIDi945041.
KEGGieco:b0383.
PATRICi32115907. VBIEscCol129921_0395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000814403.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MLXNMR-B220-310[»]
2MLYNMR-B1-150[»]
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[»]
4YR1X-ray2.24A/B31-471[»]
ProteinModelPortaliP00634.
SMRiP00634. Positions 28-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10496N.
IntActiP00634. 5 interactions.
MINTiMINT-1283619.
STRINGi511145.b0383.

Chemistry

ChEMBLiCHEMBL4217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73486; AAC73486; b0383.
BAE76164; BAE76164; BAE76164.
GeneIDi945041.
KEGGieco:b0383.
PATRICi32115907. VBIEscCol129921_0395.

Organism-specific databases

EchoBASEiEB0720.
EcoGeneiEG10727. phoA.

Phylogenomic databases

eggNOGiCOG1785.
HOGENOMiHOG000099117.
InParanoidiP00634.
KOiK01077.
OMAiEEGSQEH.
OrthoDBiEOG661H4G.
PhylomeDBiP00634.

Enzyme and pathway databases

BioCyciEcoCyc:ALKAPHOSPHA-MONOMER.
ECOL316407:JW0374-MONOMER.
MetaCyc:ALKAPHOSPHA-MONOMER.
BRENDAi3.1.3.1. 2026.
SABIO-RKP00634.

Miscellaneous databases

EvolutionaryTraceiP00634.
PROiP00634.

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]
ProtoNetiSearch...

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).
  22. "Structural basis for protein antiaggregation activity of the trigger factor chaperone."
    Saio T., Guan X., Rossi P., Economou A., Kalodimos C.G.
    Science 344:1250494-1250494(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-50; 220-310 AND 360-471 IN COMPLEX WITH TRIGGER FACTOR CHAPERONE.

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: July 22, 2015
This is version 169 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.