Reviewed,
UniProtKB/Swiss-Prot P0A9T2 (SERA_ECO57)
Last modified
June 16, 2009.
Version 35.
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=PGDH EC=1.1.1.95 | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [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-glyceric acid: 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH 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_0000076000 | |||||
Regions | |||||||||
| Domain | 338 – 409 | 72 | ACT | ||||||
Sites | |||||||||
| Active site | 240 | 1 | By similarity | ||||||
| Active site | 269 | 1 | By similarity | ||||||
| Active site | 292 | 1 | Proton donor By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG58040.1. BA000007 Genomic DNA. Translation: BAB37207.1. | |
| PIR | D85947. H91101. |
| RefSeq | NP_289481.1. NP_311811.1. |
3D structure databases | |
| SMR | P0A9T2. Positions 7-410. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 916388. 959584. |
| GenomeReviews | Gene locus Z4251 in contig AE005174_GR. Gene locus ECs3784 in contig BA000007_GR. |
| KEGG | ece:Z4251. ecs:ECs3784. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A9T2. |
| OMA | P0A9T2. GIRSKTK. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS3784-MON. |
Family and domain databases | |
| InterPro | IPR002912. ACT_bd. IPR006139. D-isomer_2_OHA_DH. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| 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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0A9T2 Secondary accession number(s): P08328, Q47633 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


