P94844 (DAPB_HELPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 89.
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: 4-hydroxy-tetrahydrodipicolinate reductase Short name=HTPA reductase EC=1.17.1.8 | ||||
| Gene names |
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| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 85962 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 254 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate By similarity. HAMAP-Rule MF_00102 |
| Catalytic activity | (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H. HAMAP-Rule MF_00102 |
| Pathway | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the DapB family. |
| Caution | Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli (PubMed:20503968) that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP lysine biosynthetic process via diaminopimelateInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase Inferred from electronic annotation. Source: InterPro NAD bindingInferred from electronic annotation. Source: HAMAP NADPH bindingInferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptorInferred 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 – 254 | 254 | 4-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102 | PRO_0000141445 | |||||
Regions | |||||||||
| Nucleotide binding | 7 – 12 | 6 | NAD(P) By similarity | ||||||
| Nucleotide binding | 91 – 93 | 3 | NAD(P) By similarity | ||||||
| Nucleotide binding | 115 – 118 | 4 | NAD(P) By similarity | ||||||
| Region | 157 – 158 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 147 | 1 | Proton donor/acceptor By similarity | ||||||
| Active site | 151 | 1 | Proton donor By similarity | ||||||
| Binding site | 35 | 1 | NADP By similarity | ||||||
| Binding site | 148 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 22 | 1 | G → E in AAB39718. Ref.1 | ||||||
| Sequence conflict | 28 | 1 | A → V in AAB39718. Ref.1 | ||||||
| Sequence conflict | 44 | 1 | S → A in AAB39718. Ref.1 | ||||||
| Sequence conflict | 76 | 1 | N → H in AAB39718. Ref.1 | ||||||
| Sequence conflict | 80 | 1 | A → T in AAB39718. Ref.1 | ||||||
| Sequence conflict | 104 | 1 | Q → K in AAB39718. Ref.1 | ||||||
| Sequence conflict | 115 | 1 | A → V in AAB39718. Ref.1 | ||||||
| Sequence conflict | 120 | 1 | I → L in AAB39718. Ref.1 | ||||||
| Sequence conflict | 132 | 1 | T → A in AAB39718. Ref.1 | ||||||
| Sequence conflict | 144 | 1 | I → V in AAB39718. Ref.1 | ||||||
| Sequence conflict | 154 | 1 | I → A in AAB39718. Ref.1 | ||||||
| Sequence conflict | 179 | 1 | I → T in AAB39718. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence of the dihydrodipicolinate reductase gene (dapB) from Helicobacter pylori and complementation in Escherichia coli." Clairoux N., Boissinot M. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 4867 / CCUG 17874 / NCTC 11638. |
| [2] | "The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C.Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U75328 Genomic DNA. Translation: AAB39718.1. AE000511 Genomic DNA. Translation: AAD07574.1. |
| PIR | F64583. |
| RefSeq | NP_207307.1. NC_000915.1. YP_006934430.1. NC_018939.1. |
3D structure databases | |
| ProteinModelPortal | P94844. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-3440N. |
| MINT | MINT-169897. |
| STRING | 85962.HP0510. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAD07574; AAD07574; HP_0510. |
| GeneID | 13869698. 900344. |
| KEGG | heo:C694_02620. hpy:HP0510. |
| PATRIC | 20592295. VBIHelPyl33062_0536. |
Phylogenomic databases | |
| eggNOG | COG0289. |
| KO | K00215. |
| OMA | FYLEGEY. |
| ProtClustDB | PRK00048. |
Enzyme and pathway databases | |
| UniPathway | UPA00034; UER00018. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| HAMAP | MF_00102. DapB. |
| InterPro | IPR022663. DapB_C. IPR000846. DapB_N. IPR022664. DapB_N_CS. IPR011770. Dihydrodipicolinate_Rdtase. IPR023940. Dihydrodipicolinate_Rdtase_bac. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR20836. PTHR20836. 1 hit. |
| Pfam | PF05173. DapB_C. 1 hit. PF01113. DapB_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000161. DHPR. 1 hit. |
| TIGRFAMs | TIGR00036. dapB. 1 hit. |
| PROSITE | PS01298. DAPB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DAPB_HELPY | ||||||||
| Accession | Primary (citable) accession number: P94844 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Helicobacter pylori Helicobacter pylori (strain 26695): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
