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: waiting to be named.

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 6: Proline dehydrogenase

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 11 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
Proline dehydrogenase activity GO:0004657
Catalysis of the reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
2 O43272 (/EXP) O43272 (/EXP)
Proline dehydrogenase activity GO:0004657
Catalysis of the reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
2 O43272 (/IDA) O43272 (/IDA)
Proline dehydrogenase activity GO:0004657
Catalysis of the reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
2 A0A0G2K2S1 (/IMP) F1MAR6 (/IMP)
Proline dehydrogenase activity GO:0004657
Catalysis of the reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
2 Q148G5 (/ISS) Q9WU79 (/ISS)
Proline dehydrogenase activity GO:0004657
Catalysis of the reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
2 O43272 (/TAS) O43272 (/TAS)
Amino acid binding GO:0016597
Interacting selectively and non-covalently with an amino acid, organic acids containing one or more amino substituents.
2 A0A0G2K2S1 (/IMP) F1MAR6 (/IMP)
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.
2 O43272 (/IDA) O43272 (/IDA)
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.
2 Q148G5 (/ISS) Q9WU79 (/ISS)
Proline dehydrogenase activity GO:0004657
Catalysis of the reaction: L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
1 Q9WU79 (/ISO)
Amino acid binding GO:0016597
Interacting selectively and non-covalently with an amino acid, organic acids containing one or more amino substituents.
1 Q9WU79 (/ISO)
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 Q9WU79 (/ISO)

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
Proline metabolic process GO:0006560
The chemical reactions and pathways involving proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
2 O43272 (/TAS) O43272 (/TAS)
Proline catabolic process GO:0006562
The chemical reactions and pathways resulting in the breakdown of proline (pyrrolidine-2-carboxylic acid), a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
2 O43272 (/TAS) O43272 (/TAS)
Intrinsic apoptotic signaling pathway in response to oxidative stress GO:0008631
A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, and ends when the execution phase of apoptosis is triggered.
2 O43272 (/NAS) O43272 (/NAS)
Positive regulation of cell death GO:0010942
Any process that increases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death.
2 O43272 (/IDA) O43272 (/IDA)
4-hydroxyproline catabolic process GO:0019470
The chemical reactions and pathways resulting in the breakdown of 4-hydroxyproline, C5H9NO3, a derivative of the amino acid proline.
2 O43272 (/TAS) O43272 (/TAS)

There are 5 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.
3 A0A0G2K2S1 (/IDA) F1MAR6 (/IDA) Q9WU79 (/IDA)
Mitochondrial inner membrane GO:0005743
The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
2 O43272 (/TAS) O43272 (/TAS)
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 Q9WU79 (/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.
1 Q9WU79 (/ISO)
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 Q9WU79 (/HDA)