Reviewed,
UniProtKB/Swiss-Prot O08651 (SERA_RAT)
Last modified
June 16, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-3-phosphoglycerate dehydrogenase Short name=3-PGDH EC=1.1.1.95 | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 533 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH. 2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH. |
| Pathway | Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glyceric acid: step 1/3. |
| Subunit structure | Homotetramer. |
| Tissue specificity | Liver, kidney, brain, testis. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Serine biosynthesis |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | L-serine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro phosphoglycerate dehydrogenase activity Ref.1Inferred from direct assay. Source: RGD |
| 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 – 533 | 532 | D-3-phosphoglycerate dehydrogenase | PRO_0000076016 | |||||
Sites | |||||||||
| Active site | 236 | 1 | By similarity | ||||||
| Active site | 265 | 1 | By similarity | ||||||
| Active site | 283 | 1 | Proton donor By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 371 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase." Achouri Y., Rider M.H., van Schaftingen E., Robbi M. Biochem. J. 323:365-370(1997) [PubMed: 9163325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Structure and chromosomal localization of the rat gene encoding 3-phosphoglycerate dehydrogenase." Robbi M., Achouri Y., Szpirer C., Van Schaftingen E. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
| [4] | Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 34-54; 248-270; 271-289 AND 365-380, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord. |
Cross-references
Sequence databases | |
|---|---|
| X97772 mRNA. Translation: CAA66374.1. AJ271975 Genomic DNA. Translation: CAB89828.1. BC086327 mRNA. Translation: AAH86327.1. | |
| IPI | IPI00475835. |
| RefSeq | NP_113808.1. |
| UniGene | Rn.6872 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HL3 based on UniProtKB Q9Z2F5. |
| SMR | O08651. Positions 5-306, 6-307. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | O08651. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000019328. Rattus norvegicus. [Contig view] |
| GeneID | 58835. |
| KEGG | rno:58835. |
| NMPDR | fig|10116.3.peg.16688. |
Organism-specific databases | |
| RGD | 61987. Phgdh. |
Phylogenomic databases | |
| HOVERGEN | O08651. |
| OMA | O08651. VEQMPLE. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-10261. |
| BRENDA | 1.1.1.95. 248. |
Gene expression databases | |
| ArrayExpress | O08651. |
| GermOnline | ENSRNOG00000019328. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR006236. D-3-Phosphoglycerate_DH. IPR006139. D-isomer_2_OHA_DH. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR015508. D3PG_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR10996:SF20. D3PG_Deh. 1 hit. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01327. PGDH. 1 hit. |
| PROSITE | PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. 1 hit. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 611397. |
Entry information
| Entry name | SERA_RAT | ||||||||
| Accession | Primary (citable) accession number: O08651 Secondary accession number(s): Q546Q9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


