P0A9T1 (SERA_ECOL6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 54.
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: D-3-phosphoglycerate dehydrogenase Short name=PGDH EC=1.1.1.95 | ||||
| Gene names |
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| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 217992 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 410 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | 3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH. 2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH. |
| Enzyme regulation | In bacteria displays feedback inhibition by L-serine By similarity. |
| Pathway | Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. Contains 1 ACT domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Serine biosynthesis |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | L-serine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD binding Inferred from electronic annotation. Source: InterPro amino acid bindingInferred from electronic annotation. Source: InterPro phosphoglycerate dehydrogenase 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 – 410 | 409 | D-3-phosphoglycerate dehydrogenase | PRO_0000076001 | |||||
Regions | |||||||||
| Domain | 338 – 409 | 72 | ACT | ||||||
| Nucleotide binding | 161 – 162 | 2 | NAD By similarity | ||||||
| Nucleotide binding | 238 – 240 | 3 | NAD By similarity | ||||||
| Nucleotide binding | 292 – 295 | 4 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 240 | 1 | By similarity | ||||||
| Active site | 269 | 1 | By similarity | ||||||
| Active site | 292 | 1 | Proton donor By similarity | ||||||
| Binding site | 181 | 1 | NAD By similarity | ||||||
| Binding site | 264 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014075 Genomic DNA. Translation: AAN81942.1. |
| RefSeq | NP_755369.1. NC_004431.1. |
3D structure databases | |
| ProteinModelPortal | P0A9T1. |
| SMR | P0A9T1. Positions 5-410. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000040402; EBESCP00000038751; EBESCG00000039452. |
| GeneID | 1039390. |
| GenomeReviews | Gene locus c3494 in contig AE014075_GR. |
| KEGG | ecc:c3494. |
| PATRIC | 18284808. VBIEscCol75197_3289. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009079. |
| HOGENOM | HBG731446. |
| OMA | RGGWLKS. |
| ProtClustDB | PRK11790. |
Family and domain databases | |
| InterPro | IPR002912. ACT-bd. IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 2 hits. |
| KO | K00058. |
| Pfam | PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. PF01842. ACT. 1 hit. [Graphical view] |
| 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... |
Entry information
| Entry name | SERA_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P0A9T1 Secondary accession number(s): P08328, Q47633 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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