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ECOLI:CATE
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | katE | |
Protein Name(s) | Catalase HPII
Hydroxyperoxidase II | |
External Links | ||
UniProt | P21179 | |
EMBL | M55161 U00096 AP009048 | |
PIR | A39129 | |
RefSeq | YP_025308.1 YP_489993.1 | |
PDB | 1CF9 1GG9 1GGE 1GGF 1GGH 1GGJ 1GGK 1IPH 1P7Y 1P7Z 1P80 1P81 1QF7 1QWS 1YE9 3P9P 3P9Q 3P9R 3P9S 3PQ2 3PQ3 3PQ4 3PQ5 3PQ6 3PQ7 3PQ8 3TTT 3TTU 3TTV 3TTW 3TTX 3VU3 4BFL 4ENP 4ENQ 4ENR 4ENS 4ENT 4ENU 4ENV 4ENW | |
PDBsum | 1CF9 1GG9 1GGE 1GGF 1GGH 1GGJ 1GGK 1IPH 1P7Y 1P7Z 1P80 1P81 1QF7 1QWS 1YE9 3P9P 3P9Q 3P9R 3P9S 3PQ2 3PQ3 3PQ4 3PQ5 3PQ6 3PQ7 3PQ8 3TTT 3TTU 3TTV 3TTW 3TTX 3VU3 4BFL 4ENP 4ENQ 4ENR 4ENS 4ENT 4ENU 4ENV 4ENW | |
ProteinModelPortal | P21179 | |
SMR | P21179 | |
BioGrid | 850594 | |
DIP | DIP-10052N | |
IntAct | P21179 | |
MINT | MINT-1247982 | |
STRING | 511145.b1732 | |
PeroxiBase | 5321 | |
SWISS-2DPAGE | P21179 | |
PaxDb | P21179 | |
PRIDE | P21179 | |
EnsemblBacteria | AAT48137 BAA15513 | |
GeneID | 12934065 946234 | |
KEGG | ecj:Y75_p1707 eco:b1732 | |
PATRIC | 32118771 | |
EchoBASE | EB0504 | |
EcoGene | EG10509 | |
eggNOG | COG0753 | |
HOGENOM | HOG000087851 | |
InParanoid | P21179 | |
KO | K03781 | |
OMA | NSIDGGW | |
OrthoDB | EOG6P5Z9F | |
PhylomeDB | P21179 | |
BioCyc | EcoCyc:HYDROPEROXIDII-MONOMER ECOL316407:JW1721-MONOMER MetaCyc:HYDROPEROXIDII-MONOMER | |
SABIO-RK | P21179 | |
EvolutionaryTrace | P21179 | |
PRO | PR:P21179 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P21179 | |
GO | GO:0005737 GO:0005829 GO:0004096 GO:0020037 GO:0042802 GO:0005506 GO:0006974 GO:0042744 GO:0006972 GO:0006979 | |
Gene3D | 2.40.180.10 3.40.50.880 | |
InterPro | IPR018028 IPR020835 IPR024708 IPR024712 IPR011614 IPR002226 IPR010582 IPR029062 | |
PANTHER | PTHR11465 | |
Pfam | PF00199 PF06628 | |
PIRSF | PIRSF038927 | |
PRINTS | PR00067 | |
SMART | SM01060 | |
SUPFAM | SSF52317 SSF56634 | |
PROSITE | PS00437 PS00438 PS51402 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004096 |
catalase activity |
ECO:0000315 |
F |
Fig. 3 Deletions show reduced catalase activity |
complete | |||||
enables |
GO:0004096 |
catalase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042744 |
hydrogen peroxide catabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10509 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0020037 |
heme binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10509 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006979 |
response to oxidative stress |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10509 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005829 |
cytosol |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10509 |
C |
Seeded From UniProt |
complete | ||
enables |
GO:0004096 |
catalase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10509 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042802 |
identical protein binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042744 |
hydrogen peroxide catabolic process |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0020037 |
heme binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006979 |
response to oxidative stress |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
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 | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0005506 |
iron ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004096 |
catalase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006972 |
hyperosmotic response |
ECO:0000270 |
expression pattern evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004096 |
catalase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004096 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004096 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004096 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004096 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004096 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004601 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0098869 |
cellular oxidant detoxification |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0004096 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0004096 |
catalase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR011614 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006979 |
response to oxidative stress |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0020037 |
heme binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR002226 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR011614 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0004096 |
catalase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042744 |
hydrogen peroxide catabolic process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0004601 |
peroxidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
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 Li, Y & Schellhorn, HE (2007) Rapid kinetic microassay for catalase activity. J Biomol Tech 18 185-7 PubMed GONUTS page
- ↑ 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
- ↑ 5.0 5.1 5.2 Loewen, PC (1984) Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity. J. Bacteriol. 157 622-6 PubMed GONUTS page
- ↑ 6.0 6.1 6.2 Bravo, J et al. (1995) Crystal structure of catalase HPII from Escherichia coli. Structure 3 491-502 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
- ↑ Heimberger, A & Eisenstark, A (1988) Compartmentalization of catalases in Escherichia coli. Biochem. Biophys. Res. Commun. 154 392-7 PubMed GONUTS page
- ↑ Weber, A et al. (2006) Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli. J. Bacteriol. 188 7165-75 PubMed GONUTS page
- ↑ Loewen, PC & Switala, J (1986) Purification and characterization of catalase HPII from Escherichia coli K12. Biochem. Cell Biol. 64 638-46 PubMed GONUTS page