Summary: Proline dehydrogenase
Proline dehydrogenase Provide feedback
No Pfam abstract.
Ling M, Allen SW, Wood JM; , J Mol Biol 1994;243:950-956.: Sequence analysis identifies the proline dehydrogenase and delta 1- pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein. PUBMED:7966312 EPMC:7966312
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002872The proline oxidase/dehydrogenase EC is responsible for the first step in the conversion of proline to glutamate for use as a carbon and nitrogen source. The enzyme requires FAD as a cofactor, and is induced by proline.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||proline dehydrogenase activity (GO:0004657)|
|Biological process||proline catabolic process (GO:0006562)|
|glutamate biosynthetic process (GO:0006537)|
|oxidation-reduction process (GO:0055114)|
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The members of this clan adopt a TIM barrel fold, which is reminiscent of flavin mononucleotide binding proteins, rather than one similar to other flavin adenine dinucleotide binding domains. However, the way the FAD cofactor binds in quite different compared to the binding of FMN in the TIM-barrel structures .
The clan contains the following 2 members:MTHFR Pro_dh
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_1092 (release 4.1)|
|Number in seed:||15|
|Number in full:||3379|
|Average length of the domain:||291.10 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||35.23 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Pro_dh domain has been found. There are 20 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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