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:

"
NAD(P)-binding Rossmann-like Domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 127: Enoyl-[acyl-carrier-protein] reductase [NADH]

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 2 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
Enoyl-[acyl-carrier-protein] reductase (NADH) activity GO:0004318
Catalysis of the reaction: acyl-
168 A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS)
(158 more)
Enoyl-[acyl-carrier-protein] reductase (NADH) activity GO:0004318
Catalysis of the reaction: acyl-
11 P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA)
(1 more)

There are 5 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
Protein homotetramerization GO:0051289
The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
94 P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA)
(84 more)
Fatty acid biosynthetic process GO:0006633
The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
85 A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS) A0A0J1I2E5 (/ISS)
(75 more)
Fatty acid elongation GO:0030497
The elongation of a fatty acid chain by the sequential addition of two-carbon units.
83 Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS) Q81GI3 (/ISS)
(73 more)
Fatty acid elongation GO:0030497
The elongation of a fatty acid chain by the sequential addition of two-carbon units.
11 P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA) P54616 (/IDA)
(1 more)
Cellular response to cold GO:0070417
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.
11 P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP) P54616 (/IEP)
(1 more)

There are 0 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.
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