Reviewed,
UniProtKB/Swiss-Prot A7MTQ2 (E4PD_VIBHB)
Last modified
June 16, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-erythrose-4-phosphate dehydrogenase Short name=E4PDH EC=1.2.1.72 | ||||
| Gene names |
| ||||
| Organism | Vibrio harveyi (strain ATCC BAA-1116 / BB120) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 338187 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 345 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate By similarity. |
| Catalytic activity | D-erythrose 4-phosphate + NAD+ + H2O = 4-phosphoerythronate + NADH. HAMAP MF_01640 |
| Pathway | Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 1/5. HAMAP MF_01640 |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Epd subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyridoxine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glucose metabolic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphate biosynthetic processInferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro erythrose-4-phosphate dehydrogenase activityInferred from electronic annotation. Source: HAMAP glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 345 | 345 | D-erythrose-4-phosphate dehydrogenase HAMAP MF_01640 | PRO_1000069898 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 12 | 2 | NAD By similarity | ||||||
| Region | 158 – 160 | 3 | Substrate binding Potential | ||||||
| Region | 217 – 218 | 2 | Substrate binding Potential | ||||||
Sites | |||||||||
| Active site | 159 | 1 | Nucleophile By similarity | ||||||
| Binding site | 204 | 1 | Substrate Potential | ||||||
| Binding site | 240 | 1 | Substrate Potential | ||||||
| Binding site | 322 | 1 | NAD By similarity | ||||||
| Site | 186 | 1 | Activates thiol group during catalysis By similarity | ||||||
Sequences
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References
| [1] | Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J., Wilson R.K. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000789 Genomic DNA. Translation: ABU72501.1. | |
| RefSeq | YP_001446728.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5554116. |
| GenomeReviews | Gene locus VIBHAR_03566 in contig CP000789_GR. |
| KEGG | vha:VIBHAR_03566. |
| NMPDR | fig|338187.4.peg.2622. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A7MTQ2. AMDLSVT. |
Family and domain databases | |
| HAMAP | MF_01640. [Tree] |
| InterPro | IPR006422. E4P_DH_bac. IPR000173. GlycerAld_3-P_DH. [Graphical view] |
| PANTHER | PTHR10836. GAP_DH. 1 hit. |
| Pfam | PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000149. GAP_DH. 1 hit. |
| PRINTS | PR00078. G3PDHDRGNASE. |
| TIGRFAMs | TIGR01532. E4PD_g-proteo. 1 hit. |
| PROSITE | PS00071. GAPDH. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | E4PD_VIBHB | ||||||||
| Accession | Primary (citable) accession number: A7MTQ2 | ||||||||
| 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


