A7YWE4 (AL4A1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 38.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial Short name=P5C dehydrogenase EC=1.5.1.12 Alternative name(s): Aldehyde dehydrogenase family 4 member A1 | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 563 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| 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 | (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Proline metabolism |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | proline biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 1-pyrroline-5-carboxylate dehydrogenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptorInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion By similarity | ||||||
| Chain | 25 – 563 | 539 | Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial | PRO_0000342182 | |||||
Regions | |||||||||
| Nucleotide binding | 296 – 301 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 314 | 1 | Proton acceptor By similarity | ||||||
| Active site | 348 | 1 | Nucleophile By similarity | ||||||
| Site | 211 | 1 | Transition state stabilizer By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 99 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 114 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 402 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 505 | 1 | Phosphotyrosine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC134524 mRNA. Translation: AAI34525.1. |
| IPI | IPI00695995. |
| RefSeq | NP_001099116.1. NM_001105646.1. |
| UniGene | Bt.3248. |
3D structure databases | |
| ProteinModelPortal | A7YWE4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7YWE4. |
Proteomic databases | |
| PRIDE | A7YWE4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000020285; ENSBTAP00000020285; ENSBTAG00000030335. |
| GeneID | 100126042. |
| KEGG | bta:100126042. |
Organism-specific databases | |
| CTD | 8659. |
Phylogenomic databases | |
| eggNOG | maNOG04501. |
| GeneTree | ENSGT00560000077335. |
| HOVERGEN | HBG050484. |
| InParanoid | A7YWE4. |
| OMA | PQSIKET. |
| OrthoDB | EOG4ZCT3Q. |
Family and domain databases | |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR005931. Delta1-pyrroline-5-COlate_DH-1. [Graphical view] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| KO | K00294. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR01236. D1pyr5carbox1. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AL4A1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: A7YWE4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with