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:
"2-enoyl-CoA Hydratase; Chain A, domain 1
".
FunFam 34: Enoyl-CoA delta isomerase 1
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 7 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 |
|---|---|---|
|
Dodecenoyl-CoA delta-isomerase activity GO:0004165
Catalysis of the reaction: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA.
|
3 | Q9VL66 (/ISS) Q9VL67 (/ISS) Q9VL68 (/ISS) |
|
Dodecenoyl-CoA delta-isomerase activity GO:0004165
Catalysis of the reaction: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA.
|
2 | P23965 (/IDA) P42125 (/IDA) |
|
Dodecenoyl-CoA delta-isomerase activity GO:0004165
Catalysis of the reaction: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA.
|
2 | P42126 (/NAS) P42126 (/NAS) |
|
Catalytic activity GO:0003824
Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
|
1 | Q57V74 (/ISM) |
|
Dodecenoyl-CoA delta-isomerase activity GO:0004165
Catalysis of the reaction: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA.
|
1 | P42125 (/ISO) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | P23965 (/IDA) |
|
Identical protein binding GO:0042802
Interacting selectively and non-covalently with an identical protein or proteins.
|
1 | P42125 (/ISO) |
There are 3 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 |
|---|---|---|
|
Fatty acid beta-oxidation GO:0006635
A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
|
3 | P23965 (/TAS) P42126 (/TAS) P42126 (/TAS) |
|
Fatty acid beta-oxidation GO:0006635
A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
|
2 | P42126 (/NAS) P42126 (/NAS) |
|
Fatty acid beta-oxidation GO:0006635
A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
|
1 | P42125 (/IMP) |
There are 13 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 |
|---|---|---|
|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
4 | P42125 (/HDA) P42126 (/HDA) P42126 (/HDA) Q9VL68 (/HDA) |
|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
4 | P23965 (/IDA) Q57V74 (/IDA) Q580R2 (/IDA) Q584L4 (/IDA) |
|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
3 | Q57V74 (/RCA) Q580R2 (/RCA) Q584L4 (/RCA) |
|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | E9ADK3 (/ISO) P42125 (/ISO) |
|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
2 | P23965 (/TAS) P42125 (/TAS) |
|
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
|
2 | P42126 (/NAS) P42126 (/NAS) |
|
Mitochondrial matrix GO:0005759
The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
|
2 | P42126 (/TAS) P42126 (/TAS) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q580R2 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | E9ADK3 (/ISO) |
|
Mitochondrion GO:0005739
A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
|
1 | Q57V74 (/ISM) |
|
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
|
1 | P42125 (/HDA) |
|
Kinetoplast GO:0020023
A sub-structure within the large single mitochondrion of kinetoplastid parasites and which is closely associated with the flagellar pocket and basal body of the flagellum.
|
1 | Q580R2 (/IDA) |
|
Kinetoplast GO:0020023
A sub-structure within the large single mitochondrion of kinetoplastid parasites and which is closely associated with the flagellar pocket and basal body of the flagellum.
|
1 | E9ADK3 (/ISO) |
