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P83155 - ALF_ANASL
- Names & Taxonomy
- Subcellular locationSubcell. location
- Pathology & BiotechPathol./Biotech
- PTM / Processing
- Family & Domains
- Entry information
- BLAST>sp|P83155|ALF_ANASL Fructose-bisphosphate aldolase (Fragment) OS=Anabaena sp. (strain L31) PE=1 SV=1 ALVPLRLLLDHAAENG
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Select a section on the left to see content.Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.By similarityD-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toiBinds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.By similarity
<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/pathway' target='_top'>More...</a></p>PathwayiCarbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
- glycolytic process Source: UniProtKB-UniPathway
<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 - Biological processiGlycolysis
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways<br/><a href='/database/170'>More..</a>UniPathwayi UPA00109; UER00183.Recommended name:Fructose-bisphosphate aldolase (EC:184.108.40.206)Short name:FBP aldolaseShort name:FBPAAlternative name(s):Fructose-1,6-bisphosphate aldolase Anabaena sp. (strain L31) 29412 [NCBI] cellular organisms › Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini 1 – ›16 ›16 Fructose-bisphosphate aldolase PRO_0000262929 Add
<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.By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toiBelongs to the class II fructose-bisphosphate aldolase family.Sequence Analysis
<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:16Mass (Da):1,702Last modified:March 1, 2002 - 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:i5D2670D9E4833A8B
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 16 – 16 1
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...
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways<br/><a href='/database/170'>More..</a> UniPathwayi UPA00109 ; UER00183 .
Family and domain databases
- Cited for: PROTEIN SEQUENCE.
ALF_ANASL P83155Primary (citable) accession number: P83155 Integrated into UniProtKB/Swiss-Prot: November 28, 2006 Last sequence update: March 1, 2002 Last modified: October 1, 2014 This is version 28 of the entry and version 1 of the sequence. [Complete history] Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program
- PATHWAY commentsIndex of metabolic and biosynthesis pathways
- SIMILARITY commentsIndex of protein domains and families
External DataDasty 3