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TableEdit
9BACT:Q1PX48
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| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status | |
|---|---|---|---|---|---|---|---|---|---|---|---|
|
public |
GO:0047991 |
hydroxylamine oxidase activity |
PMID:18397776 |
ECO:0000247 |
UniProtKB:A9ZRZ6
|
F |
Figure 3. Shows 87% sequence identity by the alignment of amino acid sequences of HAO of KSU-1 strain (HAO) and HAO of K. stuttgartiensis (Kustc1061). |
complete | |||
|
public |
GO:0019331 |
anaerobic respiration, using ammonium as electron donor |
PMID:21964329 |
ECO:0000314 |
P |
Figure 4 |
complete | ||||
|
public |
GO:0044222 |
anammoxosome |
PMID:25962914 |
ECO:0000314 |
C |
Fig 5- “ Thin sections were incubated with 1:300-diluted anti-HOX (A and B) or 1:100-diluted anti-HOX (C and D). Gold particles were visible only inside the anammoxosome. HOX appeared to be preferentially localized in the proximity of the anammoxosome membrane.” |
complete | ||||
|
protected |
involved_in |
GO:0019331 |
anaerobic respiration, using ammonium as electron donor |
PMID:21964329 |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | ||
|
protected |
enables |
GO:0047991 |
hydroxylamine oxidase activity |
GO_REF:0000003 |
ECO:0000501 |
evidence used in automatic assertion |
EC:1.7.3.4 |
F |
Seeded From UniProt |
complete | |
|
protected |
involved_in |
GO:0055114 |
oxidation-reduction process |
GO_REF:0000038 |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
UniProtKB-KW:KW-0560 |
P |
Seeded From UniProt |
complete | |
|
protected |
enables |
GO:0046872 |
metal ion binding |
GO_REF:0000038 |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
UniProtKB-KW:KW-0479 |
F |
Seeded From UniProt |
complete | |
|
protected |
enables |
GO:0016491 |
oxidoreductase activity |
GO_REF:0000038 |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
UniProtKB-KW:KW-0560 |
F |
Seeded From UniProt |
complete |
| Cancel |
