The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"FAD/NAD(P)-binding domain
".
FunFam 88: 3-phenylpropionate/cinnamic acid dioxygenase ferre...
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 12 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 |
---|---|---|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
24 |
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
P77650 (/IPI)
(14 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.
|
3 | P16640 (/IDA) P16640 (/IDA) P17052 (/IDA) |
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.
|
3 | Q9L4M8 (/ISS) X5CY81 (/ISS) X5CY81 (/ISS) |
Ferredoxin-NAD+ reductase activity GO:0008860
Catalysis of the reaction: reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH + H+.
|
2 | X5CY81 (/IDA) X5CY81 (/IDA) |
Ferredoxin-NADP+ reductase activity GO:0004324
Catalysis of the reaction: reduced ferredoxin + NADP+ = oxidized ferredoxin + NADPH + H+.
|
1 | D5IGG6 (/ISS) |
Ferredoxin-NAD+ reductase activity GO:0008860
Catalysis of the reaction: reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH + H+.
|
1 | D5IGG6 (/ISS) |
Rubredoxin-NADP reductase activity GO:0015046
Catalysis of the reaction: reduced rubredoxin + NADP+ = oxidized rubredoxin + NADPH + H+.
|
1 | P17052 (/IDA) |
Rubredoxin-NADP reductase activity GO:0015046
Catalysis of the reaction: reduced rubredoxin + NADP+ = oxidized rubredoxin + NADPH + H+.
|
1 | Q9L4M8 (/ISS) |
NADP binding GO:0050661
Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
|
1 | D5IGG6 (/ISS) |
NAD binding GO:0051287
Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
|
1 | D5IGG6 (/ISS) |
2 iron, 2 sulfur cluster binding GO:0051537
Interacting selectively and non-covalently with a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
|
1 | D5IGG6 (/ISS) |
FAD binding GO:0071949
Interacting selectively and non-covalently with the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
|
1 | D5IGG6 (/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 |
---|---|---|
3-phenylpropionate catabolic process GO:0019380
The chemical reactions and pathways resulting in the breakdown of 3-phenylpropionate, the anion of phenylpropanoic acid.
|
24 |
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
P77650 (/IMP)
(14 more) |
Carbazole catabolic process GO:0046232
The chemical reactions and pathways resulting in the breakdown of carbazole, a heterocyclic aromatic compound containing a dibenzopyrrole system that is produced during coal gasification and is present in cigarette smoke. Coal tar produced at high temperature contains an average of 1.5% carbazole. It is used widely in synthesis of dyes, pharmaceuticals, and plastics and is a suspected carcinogen.
|
1 | D5IGG6 (/IDA) |
There are 2 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 |
---|---|---|
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
9 | P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
9 | P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) P95146 (/HDA) |