Reviewed,
UniProtKB/Swiss-Prot O84375 (ARODE_CHLTR)
Last modified
June 16, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Shikimate biosynthesis protein aroDE Including the following 2 domains: 1- Recommended name: 3-dehydroquinate dehydratase Short name=3-dehydroquinase EC=4.2.1.10 Alternative name(s): Type I DHQase 2- Recommended name: Shikimate dehydrogenase EC=1.1.1.25 | ||||||
| Gene names |
| ||||||
| Organism | Chlamydia trachomatis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 813 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 478 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Bifunctional enzyme that catalyzes two sequential steps of the aromatic amino acids biosynthetic pathway. The first reaction is catalyzed by the 3-dehydroquinate dehydratase, coded by the aroD domain; the second reaction is catalyzed by the shikimate 5-dehydrogenase, coded by the aroE domain. HAMAP MF_00214 |
| Catalytic activity | 3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00214 Shikimate + NADP+ = 3-dehydroshikimate + NADPH. HAMAP MF_00214 |
| Pathway | Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 3/7. HAMAP MF_00214 |
| Sequence similarities | In the N-terminal section; belongs to the type-I 3-dehydroquinase family. In the C-terminal section; belongs to the shikimate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis |
| Ligand | NADP Schiff base |
| Molecular function | Lyase Oxidoreductase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | 3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: HAMAP NADP or NADPH bindingInferred from electronic annotation. Source: InterPro shikimate 5-dehydrogenase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 478 | 478 | Shikimate biosynthesis protein aroDE HAMAP MF_00214 | PRO_0000138824 | |||||
Regions | |||||||||
| Nucleotide binding | 337 – 341 | 5 | NADP By similarity | ||||||
| Region | 1 – 208 | 208 | 3-dehydroquinate dehydratase HAMAP MF_00214 | ||||||
| Region | 209 – 478 | 270 | Shikimate 5-dehydrogenase HAMAP MF_00214 | ||||||
| Compositional bias | 137 – 140 | 4 | Poly-Ser HAMAP MF_00214 | ||||||
Sites | |||||||||
| Active site | 110 | 1 | Proton acceptor By similarity | ||||||
| Active site | 133 | 1 | Schiff-base intermediate with substrate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx. |
Cross-references
Sequence databases | |
|---|---|
| AE001273 Genomic DNA. Translation: AAC67966.1. | |
| PIR | C71523. |
| RefSeq | NP_219879.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 884748. |
| GenomeReviews | Gene locus CT_370 in contig AE001273_GR. |
| KEGG | ctr:CT370. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O84375. |
| OMA | O84375. ISHLSHN. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:CT370-MON. |
| BRENDA | 1.1.1.25. 108. 4.2.1.10. 108. |
Family and domain databases | |
| HAMAP | MF_00214. Fused. [Tree] MF_00222. Fused. [Tree] |
| InterPro | IPR018508. 3-dehydroquinate_DH_AS. IPR013785. Aldolase_TIM. IPR001381. DHquinase_I. IPR016040. NAD(P)-bd_dom. IPR011342. Quinate/shikimate_5-DH. IPR013708. Shikimate_DH-bd_N. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01487. DHquinase_I. 1 hit. PF01488. Shikimate_DH. 1 hit. PF08501. Shikimate_dh_N. 1 hit. [Graphical view] |
| ProDom | PD005337. DHquinase_I. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00507. aroE. 1 hit. |
| PROSITE | PS01028. DEHYDROQUINASE_I. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARODE_CHLTR | ||||||||
| Accession | Primary (citable) accession number: O84375 | ||||||||
| 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


