Q1N7J3 · Q1N7J3_SPHSS
- ProteinBifunctional protein PutA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1199 (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
- H2O + L-glutamate 5-semialdehyde + NAD+ = 2 H+ + L-glutamate + NADH
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 | 791 | |||||
Sequence: E | ||||||
Active site | 825 | |||||
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas
Accessions
- Primary accessionQ1N7J3
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 | 17-64 | Proline utilization A proline dehydrogenase N-terminal | ||||
Sequence: TPLRQAITAAYRRDEAEALEPLIAAATVPDAMRDAIADTTRKLVTALR | ||||||
Domain | 72-183 | Proline dehydrogenase PutA | ||||
Sequence: VEGLVQEYALSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGDWGAHLGGEKSLFVNAATWGLVVTGKLVGSVDDRGLGAALTRLVARAGEPVIRRGVDLAMRMMGEQF | ||||||
Domain | 192-490 | Proline dehydrogenase | ||||
Sequence: ALKRAKEMEAKGFAYSYDMLGEAATTAADARRYFADYERAIHAIGKASAGRGIYAGPGISIKLSALHPRYVRAQADRVMGELLPAVKQLALLSKRYDIGFNIDAEEADRLELSLDLLESLAGDPDLAGWNGLGFVVQGYGKRCPFVIDWIIDLARRSDRRIMVRLVKGAYWDAEIKRAQVDGLPDFPVYTRKVHTDVAYIACARKLVAARDVVFPQFATHNAQTLSSIYHLAGPDFSVGDYEFQCLHGMGEPLYEQVVGAEKLNRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVNR | ||||||
Domain | 573-1009 | Aldehyde dehydrogenase | ||||
Sequence: RTVFNPADHRDVVGRVTDATEADARAAVIRAAESRWPNSAVSDRAAMLEAAADAMQARMPILLGLIVREAGKSLPNAIAEVREAIDFLRYYARQAHATFGAQQQSLGPVVCISPWNFPLAIFTGQVAAALMAGNPVLAKPAEETPLIAAESVRLLHDAGVPADALQLLPGDGGIGAALVAAPETAAVMFTGSTEVARLIQRQLAPRLSRAGRPIPLIAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLTMLKGALAELRIGRTDALSVDIGPVITAEARDGIIAHIDAMRAKGRGVEQSVLPPETAHGTFVAPTIIEIDGIADLEREVFGPVLHVLRFKREGLDALVDQINATGYGLTFGLHTRLDETIARVTSRAKVGNIYVNRNVIGAIVGVQPFGGRGLSGTGPKAGGPLYL |
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
- Length1,199
- Mass (Da)127,900
- Last updated2006-05-30 v1
- ChecksumF84EEC1CF432A81D
Keywords
- Technical term