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ECOLI:UXUA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | uxuA | |
| Protein Name(s) | Mannonate dehydratase
D-mannonate hydro-lyase | |
| External Links | ||
| UniProt | P24215 | |
| EMBL | D13329 U14003 U00096 AP009048 AJ225176 X03411 X91735 | |
| PIR | I57745 S56547 | |
| RefSeq | NP_418742.1 YP_492456.1 | |
| PDB | 4EAC 4EAY | |
| PDBsum | 4EAC 4EAY | |
| ProteinModelPortal | P24215 | |
| SMR | P24215 | |
| DIP | DIP-11108N | |
| IntAct | P24215 | |
| STRING | 511145.b4322 | |
| PaxDb | P24215 | |
| PRIDE | P24215 | |
| EnsemblBacteria | AAC77278 BAE78315 | |
| GeneID | 12932009 947082 | |
| KEGG | ecj:Y75_p4208 eco:b4322 | |
| PATRIC | 32124240 | |
| EchoBASE | EB1059 | |
| EcoGene | EG11066 | |
| eggNOG | COG1312 | |
| HOGENOM | HOG000195381 | |
| InParanoid | P24215 | |
| KO | K01686 | |
| OMA | EGDVDMY | |
| OrthoDB | EOG6ZSP6Z | |
| PhylomeDB | P24215 | |
| BioCyc | EcoCyc:MANNONDEHYDRAT-MONOMER ECOL316407:JW4285-MONOMER MetaCyc:MANNONDEHYDRAT-MONOMER | |
| UniPathway | UPA00246 | |
| PRO | PR:P24215 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P24215 | |
| GO | GO:0008198 GO:0030145 GO:0008927 GO:0006974 GO:0042840 | |
| Gene3D | 3.20.20.150 | |
| HAMAP | MF_00106 | |
| InterPro | IPR004628 IPR013022 | |
| Pfam | PF03786 | |
| PIRSF | PIRSF016049 | |
| SUPFAM | SSF51658 | |
| TIGRFAMs | TIGR00695 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0008927 |
mannonate dehydratase activity |
ECO:0000315 |
F |
Table 3 shows high mannonate hydrolyase activity by various mutants when functional uxuA gene present in the plasmid. |
complete | |||||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0042840 |
D-glucuronate catabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11066 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0030145 |
manganese ion binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11066 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11066 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0008198 |
ferrous iron binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11066 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006974 |
cellular response to DNA damage stimulus |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0042840 |
D-glucuronate catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0042840 |
D-glucuronate catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0030145 |
manganese ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008198 |
ferrous iron binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008198 |
ferrous iron binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006064 |
glucuronate catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008927 |
mannonate dehydratase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000034424 |
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 | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Ritzenthaler, P et al. (1980) Construction and expression of hybrid plasmids containing Escherichia coli K-12 uxu genes. J. Bacteriol. 143 1116-26 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed GONUTS page
- ↑ Portalier, R et al. (1980) Regulation of Escherichia coli K-12 hexuronate system genes: exu regulon. J. Bacteriol. 143 1095-107 PubMed GONUTS page
- ↑ Robert-Baudouy, JM et al. (1972) [Genetic mapping and biochemical characterization of mutations in the mannonic hydrolyase structural gene of Escherichia coli K 12]. Mol. Gen. Genet. 118 351-62 PubMed GONUTS page
- ↑ Qiu, X et al. (2012) Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium. J. Struct. Biol. 180 327-34 PubMed GONUTS page
- ↑ 7.0 7.1 Robert-Baudouy, JM & Stoeber, FR (1973) [Purification and properties of D-mannonate hydrolyase from Escherichia coli K12]. Biochim. Biophys. Acta 309 473-85 PubMed GONUTS page
- ↑ 8.0 8.1 Dreyer, JL (1987) The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases. Eur. J. Biochem. 166 623-30 PubMed GONUTS page
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