fbaA:Gene Product(s): Difference between revisions
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!align=left | !align=left {{table heading style}} |Standard name | ||
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FbaA | FbaA | ||
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!align=left | !align=left {{table heading style}} |Synonyms | ||
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fructose-bisphosphate aldolase, class II<ref name='LIB:Riley_2006'/>, B2925<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fda<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ald<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FbaA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fba<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> | fructose-bisphosphate aldolase, class II<ref name='LIB:Riley_2006'/>, B2925<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fda<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Ald<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, FbaA<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Fba<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> | ||
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!align=left | !align=left {{table heading style}} |Product description | ||
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fructose bisphosphate aldolase<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>; | fructose bisphosphate aldolase<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>; | ||
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Fructose-bisphosphate aldolase, class II; binds Zn(II); homdomeric<ref name='LIB:EcoGene'/> | Fructose-bisphosphate aldolase, class II; binds Zn(II); homdomeric<ref name='LIB:EcoGene'/> | ||
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!align=left | !align=left {{table heading style}} |EC number (for enzymes) | ||
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* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]<ref name='LIB:Riley_2006'/> | * [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]<ref name='LIB:Riley_2006'/> | ||
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{| | {| {{Prettytable}} id="Q46aac7390ab11" class=" tableEdit GO_table_product dataTable" | ||
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!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status | !|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status | ||
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!|Partner Type!!Partner!!Notes!!References!!Evidence | !|Partner Type!!Partner!!Notes!!References!!Evidence | ||
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!|Compartment!!Description!!Evidence!!Source!!Notes | !|Compartment!!Description!!Evidence!!Source!!Notes | ||
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!align=left | !align=left {{table heading style}} |Sequence | ||
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[http://biocyc.org/ECOLI/sequence-aa?object=FRUCTBISALD-CLASSII-MONOMER at EcoCyc] | [http://biocyc.org/ECOLI/sequence-aa?object=FRUCTBISALD-CLASSII-MONOMER at EcoCyc] | ||
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LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL</pre> | LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL</pre> | ||
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!align=left | !align=left {{table heading style}} |Length | ||
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359 | 359 | ||
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!align=left | !align=left {{table heading style}} |Mol. Wt | ||
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39.146 kDa | 39.146 kDa | ||
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!align=left | !align=left {{table heading style}} |pI | ||
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5.8 (calculated) | 5.8 (calculated) | ||
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!align=left | !align=left {{table heading style}} |Extinction coefficient | ||
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41,370 - 41,870 (calc based on 13 Y, 4 W, and 4 C residues) | 41,370 - 41,870 (calc based on 13 Y, 4 W, and 4 C residues) | ||
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****************************************************************************************** -->{{Product_domains_motifs_help}} | ****************************************************************************************** -->{{Product_domains_motifs_help}} | ||
{| id="I46aac743c4f74" class=" tableEdit Product_motif_table" | {| id="I46aac743c4f74" class=" tableEdit Product_motif_table dataTable" | ||
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!|Type!!Residues!!Description!!Notes | !|Type!!Residues!!Description!!Notes!!References | ||
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[http://www.uniprot.org/uniprot/P0AB71#section_features UniProt:P0AB71] | [http://www.uniprot.org/uniprot/P0AB71#section_features UniProt:P0AB71] | ||
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!align=left | !align=left {{table heading style}} |Structures | ||
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<beststructure> | <beststructure> | ||
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</beststructure> | </beststructure> | ||
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!align=left | !align=left {{table heading style}} |Models | ||
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View models at: | View models at: | ||
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Revision as of 19:50, 23 February 2010
{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>
| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
| Standard name |
FbaA |
|---|---|
| Synonyms |
fructose-bisphosphate aldolase, class II[1], B2925[2][1], Fda[2][1], Ald[2][1], FbaA[2][1], Fba[2][1] |
| Product description |
fructose bisphosphate aldolase[2][3]; Component of fructose bisphosphate aldolase class II[2][3] Fructose-bisphosphate aldolase, class II; binds Zn(II); homdomeric[4] |
| EC number (for enzymes) | |
| edit table |
Notes
Function
Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
| Qualifier | GO ID | GO term name | Reference(s) | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0046872 |
metal ion binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0016829 |
lyase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0008270 |
zinc ion binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0008152 |
metabolic process |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [5] |
complete | |||
| GO:0006096 |
glycolysis |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [5] |
complete | |||
| GO:0004332 |
fructose-bisphosphate aldolase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0003824 |
catalytic activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0005737 |
cytoplasm |
C |
Seeded from Riley et al 2006 [1]. |
required fields missing | ||||
| GO:0016052 |
carbohydrate catabolic process |
P |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0004332 |
fructose-bisphosphate aldolase activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
| GO:0006094 |
gluconeogenesis |
P |
required field missing | |||||
| GO:0004332 |
fructose-bisphosphate aldolase activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
| GO:0008270 |
zinc ion binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0004332 |
fructose-bisphosphate aldolase activity |
IMP: Inferred from Mutant Phenotype |
F |
complete | ||||
| GO:0008270 |
zinc ion binding |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| edit table |
Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
| Partner Type | Partner | Notes | References | Evidence |
|---|---|---|---|---|
|
Protein |
Subunits of fructose bisphosphate aldolase class II |
could be indirect |
||
|
Protein |
dnaK |
Experiment(s):EBI-879773, EBI-884401 | ||
|
Protein |
fldA |
Experiment(s):EBI-879773 | ||
|
Protein |
hsdR |
Experiment(s):EBI-879773 | ||
|
Protein |
rpsB |
Experiment(s):EBI-879773 | ||
|
Protein |
yfeR |
Experiment(s):EBI-879773 | ||
| edit table |
Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
| Compartment | Description | Evidence | Source | Notes |
|---|---|---|---|---|
|
Cytoplasm |
| |||
| edit table |
Notes
Structure and Physical Properties
Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
| Sequence |
MSKIFDFVKP GVITGDDVQK VFQVAKENNF ALPAVNCVGT DSINAVLETA AKVKAPVIVQ FSNGGASFIA GKGVKSDVPQ GAAILGAISG AHHVHQMAEH YGVPVILHTD HCAKKLLPWI DGLLDAGEKH FAATGKPLFS SHMIDLSEES LQENIEICSK YLERMSKIGM TLEIELGCTG GEEDGVDNSH MDASALYTQP EDVDYAYTEL SKISPRFTIA ASFGNVHGVY KPGNVVLTPT ILRDSQEYVS KKHNLPHNSL NFVFHGGSGS TAQEIKDSVS YGVVKMNIDT DTQWATWEGV LNYYKANEAY LQGQLGNPKG EDQPNKKYYD PRVWLRAGQT SMIARLEKAF QELNAIDVL |
|---|---|
| Length |
359 |
| Mol. Wt |
39.146 kDa |
| pI |
5.8 (calculated) |
| Extinction coefficient |
41,370 - 41,870 (calc based on 13 Y, 4 W, and 4 C residues) |
| edit table |
Domains/Motifs/Modification Sites
|
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
|
<motif_map/> |
|
Structure
|
Structure figures
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
| Resource type | Source | Notes/Reference |
|---|---|---|
| edit table |
Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
| Database | Accession | Notes |
|---|---|---|
|
| ||
| edit table |
Notes
Links
| Name | URL | Comments |
|---|---|---|
| edit table |
References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
- ↑ EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
- ↑ 8.0 8.1 8.2 Böck, A & Neidhardt, FC (1966) Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity. J. Bacteriol. 92 464-9 PubMed
- ↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed
- ↑ Berry, A & Marshall, KE (1993) Identification of zinc-binding ligands in the class II fructose-1,6-bisphosphate aldolase of Escherichia coli. FEBS Lett. 318 11-6 PubMed
- ↑ Alefounder, PR et al. (1989) Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Biochem. J. 257 529-34 PubMed
Categories
- GO:0046872 ! metal ion binding
- GO:0016829 ! lyase activity
- GO:0008270 ! zinc ion binding
- GO:0008152 ! metabolic process
- GO:0006096 ! glycolytic process
- GO:0004332 ! fructose-bisphosphate aldolase activity
- GO:0003824 ! catalytic activity
- GO:0005515 ! protein binding
- GO:0005737 ! cytoplasm
- GO:0016052 ! carbohydrate catabolic process
- GO:0006094 ! gluconeogenesis
- Proteins
- Complex:fructose bisphosphate aldolase class II
- Products with structures in PDB