Q5RAQ3 (P5CR2_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 44.
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: Pyrroline-5-carboxylate reductase 2 Short name=P5C reductase 2 Short name=P5CR 2 EC=1.5.1.2 | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 320 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 | Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP+. Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH By similarity. |
| Catalytic activity | L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H. |
| Pathway | |
| Subunit structure | Homodecamer; composed of 5 homodimers By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the pyrroline-5-carboxylate reductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Proline biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorInferred from electronic annotation. Source: InterPro pyrroline-5-carboxylate reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 320 | 319 | Pyrroline-5-carboxylate reductase 2 | PRO_0000187319 | |||||
Regions | |||||||||
| Nucleotide binding | 6 – 11 | 6 | NADP By similarity | ||||||
| Nucleotide binding | 69 – 72 | 4 | NADP By similarity | ||||||
| Nucleotide binding | 95 – 97 | 3 | NADP By similarity | ||||||
Sites | |||||||||
| Binding site | 34 | 1 | NADP; via carbonyl oxygen By similarity | ||||||
| Binding site | 56 | 1 | NADP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 303 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 304 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR858959 mRNA. Translation: CAH91157.1. |
| RefSeq | NP_001125676.1. NM_001132204.1. |
| UniGene | Pab.9228. |
3D structure databases | |
| ProteinModelPortal | Q5RAQ3. |
| SMR | Q5RAQ3. Positions 1-275. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100172597. |
| KEGG | pon:100172597. |
Organism-specific databases | |
| CTD | 29920. |
Phylogenomic databases | |
| HOVERGEN | HBG053399. |
Family and domain databases | |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR016040. NAD(P)-bd_dom. IPR004455. NADP_OxRdtase_F420. IPR000304. Pyrroline-COOH_reductase. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00286. |
| PANTHER | PTHR11645. P5CR. 1 hit. |
| Pfam | PF03807. F420_oxidored. 1 hit. [Graphical view] |
| PIRSF | PIRSF000193. Pyrrol-5-carb_rd. 1 hit. |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| TIGRFAMs | TIGR00112. ProC. 1 hit. |
| PROSITE | PS00521. P5CR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | P5CR2_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RAQ3 | ||||||||
| 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