CATH Superfamily 1.20.58.100
Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain
The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain
".
FunFam 2: L-aspartate oxidase
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 5 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
L-aspartate oxidase activity GO:0008734
Catalysis of the reaction: L-aspartate + O2 = iminosuccinate + hydrogen peroxide.
|
14 |
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
(4 more) |
L-aspartate oxidase activity GO:0008734
Catalysis of the reaction: L-aspartate + O2 = iminosuccinate + hydrogen peroxide.
|
14 |
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
(4 more) |
L-aspartate:fumarate oxidoreductase activity GO:0044318
Catalysis of the reaction: L-aspartate + fumarate = alpha-iminosuccinate + succinate.
|
14 |
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
(4 more) |
Flavin adenine dinucleotide binding GO:0050660
Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
|
14 |
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
(4 more) |
L-aspartate oxidase activity GO:0008734
Catalysis of the reaction: L-aspartate + O2 = iminosuccinate + hydrogen peroxide.
|
2 | Q9KPA4 (/ISS) Q9KPA4 (/ISS) |
There are 2 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
'de novo' NAD biosynthetic process from aspartate GO:0034628
The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD), beginning with the synthesis of aspartate from simpler precursors; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH.
|
14 |
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
P10902 (/IMP)
(4 more) |
NADH metabolic process GO:0006734
The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
|
2 | Q9KPA4 (/ISS) Q9KPA4 (/ISS) |
There are 1 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
14 |
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
P10902 (/IDA)
(4 more) |