Q8CHT0 · AL4A1_MOUSE
- ProteinDelta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- GeneAldh4a1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids562 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity).
Catalytic activity
- H2O + L-glutamate 5-semialdehyde + NAD+ = 2 H+ + L-glutamate + NADH
Pathway
Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 207 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Site | 210 | Transition state stabilizer | ||||
Sequence: N | ||||||
Binding site | 232 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 285-289 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSVPT | ||||||
Active site | 313 | Proton acceptor | ||||
Sequence: E | ||||||
Active site | 347 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 446 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 512 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | 1-pyrroline-5-carboxylate dehydrogenase activity | |
Molecular Function | aldehyde dehydrogenase (NAD+) activity | |
Molecular Function | identical protein binding | |
Biological Process | proline catabolic process to glutamate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDelta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- EC number
- Short namesP5C dehydrogenase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8CHT0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-23 | Mitochondrion | ||||
Sequence: MLPLPSLRRSLLSHAWRGAGLRW | ||||||
Chain | PRO_0000007174 | 24-562 | Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial | |||
Sequence: KHTSSLKVTNEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYGLTGAVFAQDKAIVQEATRMLRNAAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWRYSYMQ | ||||||
Modified residue | 30 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 43 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 51 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 92 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 92 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 98 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 98 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 113 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 113 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 129 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 129 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 174 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 174 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 317 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 346 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 357 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 357 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 364 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 375 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 394 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 461 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 508 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 508 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 530 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 551 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length562
- Mass (Da)61,841
- Last updated2011-07-27 v3
- Checksum4D8A0C9C68A99478
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 18 | in Ref. 1; BAC32045 and 4; AAH56226/AAH39281/AAH24133 | ||||
Sequence: G → S | ||||||
Sequence conflict | 32 | in Ref. 1; BAC32045 and 4; AAH56226/AAH39281/AAH24133 | ||||
Sequence: T → A | ||||||
Sequence conflict | 47 | in Ref. 1; BAC32045 | ||||
Sequence: D → G | ||||||
Sequence conflict | 60 | in Ref. 1; BAC32045 and 4; AAH56226/AAH39281/AAH24133 | ||||
Sequence: M → T | ||||||
Sequence conflict | 467 | in Ref. 1; BAC32045 and 4; AAH56226/AAH39281/AAH24133/AAH26589 | ||||
Sequence: Q → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK044712 EMBL· GenBank· DDBJ | BAC32045.1 EMBL· GenBank· DDBJ | mRNA | ||
AL831790 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466615 EMBL· GenBank· DDBJ | EDL13315.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC024133 EMBL· GenBank· DDBJ | AAH24133.1 EMBL· GenBank· DDBJ | mRNA | ||
BC026589 EMBL· GenBank· DDBJ | AAH26589.1 EMBL· GenBank· DDBJ | mRNA | ||
BC039281 EMBL· GenBank· DDBJ | AAH39281.2 EMBL· GenBank· DDBJ | mRNA | ||
BC056226 EMBL· GenBank· DDBJ | AAH56226.1 EMBL· GenBank· DDBJ | mRNA |