Q87F49 (DAPE_XYLFT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
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: Succinyl-diaminopimelate desuccinylase Short name=SDAP desuccinylase EC=3.5.1.18 Alternative name(s): N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase | ||||
| Gene names |
| ||||
| Organism | Xylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 183190 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella › ![]() |
Protein attributes
| Sequence length | 377 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls By similarity. HAMAP-Rule MF_01690 |
| Catalytic activity | N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate. HAMAP-Rule MF_01690 |
| Cofactor | Binds 1 Zn2+ ion per subunit By similarity. Binds 1 Co2+ ion per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3. HAMAP-Rule MF_01690 |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the peptidase M20A family. DapE subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Ligand | Cobalt Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete 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 proteolysisInferred from electronic annotation. Source: InterPro |
| Molecular_function | cobalt ion binding Inferred from electronic annotation. Source: HAMAP metallopeptidase activityInferred from electronic annotation. Source: InterPro succinyl-diaminopimelate desuccinylase activityInferred from electronic annotation. Source: HAMAP zinc ion bindingInferred 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 – 377 | 377 | Succinyl-diaminopimelate desuccinylase HAMAP-Rule MF_01690 | PRO_0000375792 | |||||
Sites | |||||||||
| Active site | 68 | 1 | By similarity | ||||||
| Active site | 133 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 66 | 1 | Cobalt or zinc 1 By similarity | ||||||
| Metal binding | 99 | 1 | Cobalt or zinc 1 By similarity | ||||||
| Metal binding | 99 | 1 | Cobalt or zinc 2 By similarity | ||||||
| Metal binding | 134 | 1 | Cobalt or zinc 2 By similarity | ||||||
| Metal binding | 162 | 1 | Cobalt or zinc 1 By similarity | ||||||
| Metal binding | 348 | 1 | Cobalt or zinc 2 By similarity | ||||||
Sequences
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References
| [1] | "Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa." Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M. Kitajima J.P.J. Bacteriol. 185:1018-1026(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Temecula1 / ATCC 700964. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE009442 Genomic DNA. Translation: AAO27988.1. |
| RefSeq | NP_778339.1. NC_004556.1. |
3D structure databases | |
| ProteinModelPortal | Q87F49. |
| SMR | Q87F49. Positions 2-374. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 183190.PD0088. |
Protein family/group databases | |
| MEROPS | M20.010. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAO27988; AAO27988; PD_0088. |
| GeneID | 1144300. |
| KEGG | xft:PD0088. |
| PATRIC | 24147572. VBIXylFas71109_0122. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0624. |
| KO | K01439. |
| OMA | MWARRGN. |
| ProtClustDB | PRK13009. |
Enzyme and pathway databases | |
| UniPathway | UPA00034; UER00021. |
Family and domain databases | |
| HAMAP | MF_01690. DapE. |
| InterPro | IPR001261. ArgE/DapE_CS. IPR005941. DapE_proteobac. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view] |
| Pfam | PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view] |
| SUPFAM | SSF55031. Peptidase_M20_dimer. 1 hit. |
| TIGRFAMs | TIGR01246. dapE_proteo. 1 hit. |
| PROSITE | PS00758. ARGE_DAPE_CPG2_1. False negative. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DAPE_XYLFT | ||||||||
| Accession | Primary (citable) accession number: Q87F49 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
