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P81800 - PPB1_PREIN
- Names & Taxonomy
- Subcellular locationSubcell. location
- Pathology & BiotechPathol./Biotech
- PTM / Processing
- Family & Domains
- Entry information
- BLAST>sp|P81800|PPB1_PREIN Alkaline phosphatase (Fragment) OS=Prevotella intermedia PE=1 SV=1 TDMLAVSVSSTDAIGHKYGT
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Select a section on the left to see content.Acts against tyrosine-phosphatases.CuratedA phosphate monoester + H2O = an alcohol + phosphate.
<p>Describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.</p><p><a href='../manual/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationiCompletely inhibited by thiol-reducing agents, such as DTT and 2-mercaptoethanol. Activity was also inhibited by sodium orthovanadate, sodium molybdate, N-ethylmaleimide, EDTA and zinc ion, but was not inhibited by okadaic acid.
- alkaline phosphatase activity Source: UniProtKB
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> Inferred from direct assayi
Recommended name:Alkaline phosphatase (EC:220.127.116.11)Short name:ALPaseAlternative name(s):PiALP
- dephosphorylation Source: GOC
- metabolic process Source: UniProtKB
Prevotella intermediaCurated 28131 [NCBI] cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Bacteroidia › Bacteroidales › Prevotellaceae › Prevotella
Feature key Position(s) Length Description Graphical view Feature identifier Actions ‹1 – ›20 ›20 Alkaline phosphatase PRO_0000058533 Add
<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationiThe N-terminus is blocked.
<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMiDisulfide bond
<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureiHomodimer; may be disulfide-linked.Curated
<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusi: Fragment.Length:20Mass (Da):2,053Last modified:June 1, 2001 - v1<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA8D8A9276AE0ED83
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.</p><p><a href='../manual/non_ter' target='_top'>More...</a></p>Non-terminal residuei 1 – 1 1 Curated <p>Is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.</p><p><a href='../manual/non_ter' target='_top'>More...</a></p>Non-terminal residuei 20 – 20 1 Curated
3D structure databases
Database of comparative protein structure models<br/><a href='/database/63'>More..</a> ModBasei Search... Search...
Protocols and materials databases
Structural Biology Knowledgebase Search...
Family and domain databases
- "Purification and characterization of alkaline phosphatase containing phosphotyrosyl phosphatase activity from the bacterium Prevotella intermedia."
Ansai T., Awano S., Chen X., Fuchi T., Arimoto T., Akifusa S., Takehara T.
FEBS Lett. 428:157-160(1998) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE, CHARACTERIZATION.Strain: ATCC 25611 / DSM 20706 / JCM 12248 / NCTC 13070 / VPI 4197.
PPB1_PREIN P81800Primary (citable) accession number: P81800 Integrated into UniProtKB/Swiss-Prot: May 10, 2004 Last sequence update: June 1, 2001 Last modified: October 1, 2014 This is version 32 of the entry and version 1 of the sequence. [Complete history] Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program
External DataDasty 3