D4ZFQ1 · D4ZFQ1_SHEVD
- ProteinBifunctional protein PutA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1064 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Oxidizes proline to glutamate for use as a carbon and nitrogen source.
Catalytic activity
- L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + 2 H+
Cofactor
Pathway
Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 816 | |||||
Sequence: E | ||||||
Active site | 850 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic side of plasma membrane | |
Molecular Function | 1-pyrroline-5-carboxylate dehydrogenase activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | proline dehydrogenase activity | |
Biological Process | proline biosynthetic process | |
Biological Process | proline catabolic process to glutamate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein PutA
Including 2 domains:
- Recommended nameProline dehydrogenase
- EC number
- Alternative names
- Recommended nameDelta-1-pyrroline-5-carboxylate dehydrogenase
- EC number
- Short namesP5C dehydrogenase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Alteromonadales > Shewanellaceae > Shewanella
Accessions
- Primary accessionD4ZFQ1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 81-194 | Proline dehydrogenase PutA | ||||
Sequence: IDAFLQQYSLETQEGIILMCLAEALLRIPDAATADALIEDKLSGAKWDIHLSKSDSILVNASTWGLMLTGKIVKLDRNIDGKPSSLLNRLVNRMGEPVIRQAMLAAMKIMGKQF | ||||||
Domain | 204-498 | Proline dehydrogenase | ||||
Sequence: LKNSLDKRKLGYTHSYDMLGEAALTKTDAQKYFEDYSSAIASLGEQSYDESQAPRPTISIKLSALHPRYEVANEDRTLTELYDTLIKLIQQARGVNIGISIDAEEMDRLELSLKLFQKLFNSDAAKGWGVLGIVVQAYSKRALPVLCWLTRLSKDQGDEIPVRLVKGAYWDSELKWGQEKGEAGYPLFTRKAGTDVSYLACARYLLSDATRGAIYPQFASHNAQTVASITDMAGDRNYEFQRLHGMGEELYDTLLAESGVKTVRIYAPVGAHKDLLPYLVRRLLENGANTSFVHK | ||||||
Domain | 582-1042 | Aldehyde dehydrogenase | ||||
Sequence: ETNEVVSPYDTTQVVGKLAFANNQAIEQALTGADAAFSGWCNTPVEVRANALQKLADLLEENREELIALCTREAGKSIQDGIDEVREAVDFCRYYAVQAKKMMAQPELLPGPTGELNELFLQGRGIFVCISPWNFPLAIFLGQVAAALAAGNTVVAKPAEQTSIVGFRAVQLAHQAGIPKDVLQFLPGTGATVGAAITSDERIAGVCFTGSTGTAKLINRTLANREGAIIPLIAETGGQNAMVVDSTSQPEQVVNDVVASSFTSAGQRCSALRVLFLQEDIADRVLEVLKGAMDELSIGNPSSIKTDVGPVIDAMAKANLNAHIDHIKQVGTLLKQLELPAGTDKGHFVAPTAVEIDSIKVLEKEHFGPILHVIRYKASELAKVIDEINSTGFGLTLGIHSRNEGHALKIASKVNVGNVYINRNQIGAVVGVQPFGGQGLSGTGPKAGGPHYLTRFITEKT |
Sequence similarities
In the C-terminal section; belongs to the aldehyde dehydrogenase family.
In the N-terminal section; belongs to the proline dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,064
- Mass (Da)115,898
- Last updated2010-06-15 v1
- Checksum88DE9CEA15692436
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP011177 EMBL· GenBank· DDBJ | BAJ00500.1 EMBL· GenBank· DDBJ | Genomic DNA |