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MYCTU:ALF
Contents
| Species (Taxon ID) | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332) | |
| Gene Name(s) | fba | |
| Protein Name(s) | Fructose-bisphosphate aldolase
FBP aldolase FBPA Fructose-1,6-bisphosphate aldolase | |
| External Links | ||
| UniProt | P9WQA3 | |
| EMBL | AL123456 | |
| PIR | D70576 | |
| RefSeq | NP_214877.1 YP_006513689.1 | |
| PDB | 3EKL 3EKZ 3ELF 4A21 4A22 4DEF 4DEL 4LV4 | |
| PDBsum | 3EKL 3EKZ 3ELF 4A21 4A22 4DEF 4DEL 4LV4 | |
| ProteinModelPortal | P9WQA3 | |
| SMR | P9WQA3 | |
| BindingDB | P9WQA3 | |
| ChEMBL | CHEMBL1287620 | |
| GeneID | 13318230 886474 | |
| KEGG | mtu:Rv0363c mtv:RVBD_0363c | |
| TubercuList | Rv0363c | |
| KO | K01624 | |
| OMA | RMSKMGM | |
| PhylomeDB | P9WQA3 | |
| UniPathway | UPA00109 | |
| Proteomes | UP000001584 | |
| GO | GO:0005618 GO:0005576 GO:0005886 GO:0004332 GO:0008270 GO:0006096 | |
| Gene3D | 3.20.20.70 | |
| InterPro | IPR013785 IPR006411 IPR000771 | |
| Pfam | PF01116 | |
| PIRSF | PIRSF001359 | |
| TIGRFAMs | TIGR00167 TIGR01520 | |
| PROSITE | PS00602 PS00806 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0006096 |
glycolysis |
ECO:0000314 |
P |
Immunohistochemistry detected FBA-tb using polyclonal anti-FBA-tb antibodies and tyramide amplification signal in figure 3. |
complete | |||||
| GO:0042132 |
fructose 1,6-bisphosphate 1-phosphatase activity |
ECO:0000315 |
F |
The kinetic constants for recombinant wild-type aldolase B were obtained in the same fashion as for the mutant enzymes shown in Table 2. |
complete | |||||
| GO:0045820 |
negative regulation of glycolysis |
ECO:0000314 |
P |
See supplemental Fig. S4. |
complete | |||||
|
enables |
GO:0035375 |
zymogen binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005618 |
cell wall |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002412655 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002412655 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002412655 |
C |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005618 |
cell wall |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002412655 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN002412655 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0003824 |
catalytic activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0005975 |
carbohydrate metabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016832 |
aldehyde-lyase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004332 |
fructose-bisphosphate aldolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016829 |
lyase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006096 |
glycolytic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0324 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 de la Paz Santangelo, M et al. (2011) Glycolytic and non-glycolytic functions of Mycobacterium tuberculosis fructose-1,6-bisphosphate aldolase, an essential enzyme produced by replicating and non-replicating bacilli. J. Biol. Chem. 286 40219-31 PubMed GONUTS page
- ↑ Pezza, JA et al. (2003) Spatial clustering of isozyme-specific residues reveals unlikely determinants of isozyme specificity in fructose-1,6-bisphosphate aldolase. J. Biol. Chem. 278 17307-13 PubMed GONUTS page
- ↑ 3.0 3.1 Xolalpa, W et al. (2007) Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis. Proteomics 7 3332-41 PubMed GONUTS page
- ↑ Gu, S et al. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2 1284-96 PubMed GONUTS page
- ↑ Wolfe, LM et al. (2010) Proteomic definition of the cell wall of Mycobacterium tuberculosis. J. Proteome Res. 9 5816-26 PubMed GONUTS page
- ↑ Målen, H et al. (2007) Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7 1702-18 PubMed GONUTS page
- ↑ 7.0 7.1 7.2 Ramsaywak, PC et al. (2004) Molecular cloning, expression, purification, and characterization of fructose 1,6-bisphosphate aldolase from Mycobacterium tuberculosis--a novel Class II A tetramer. Protein Expr. Purif. 37 220-8 PubMed GONUTS page
- ↑ 8.0 8.1 8.2 8.3 8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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