Q62GA0 (Q62GA0_BURMA) Unreviewed, UniProtKB/TrEMBL
Last modified
May 16, 2012.
Version 53.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Diaminopimelate decarboxylase HAMAP MF_02120 Short name=DAP decarboxylase HAMAP MF_02120 Short name=DAPDC HAMAP MF_02120 EC=4.1.1.20 HAMAP MF_02120 | ||||
| Gene names |
| ||||
| Organism | Burkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 13373 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group |
Protein attributes
| Sequence length | 423 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine By similarity. HAMAP MF_02120 |
| Catalytic activity | Meso-2,6-diaminoheptanedioate = L-lysine + CO2. HAMAP MF_02120 RuleBase RU003738 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_02120 RuleBase RU003738 SAAS SAAS000183 |
| Pathway | Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. HAMAP MF_02120 RuleBase RU003738 |
| Subunit structure | Homodimer By similarity. HAMAP MF_02120 |
| Sequence similarities | Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily. HAMAP MF_02120 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Lysine biosynthesis HAMAP MF_02120 RuleBase RU003738 |
| Ligand | Pyridoxal phosphate HAMAP MF_02120 SAAS SAAS000183 |
| Molecular function | Decarboxylase HAMAP MF_02120 SAAS SAAS009006 RuleBase RU003738 Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP |
| Molecular function | diaminopimelate decarboxylase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Region | 278 – 281 | 4 | Pyridoxal phosphate binding By similarity HAMAP MF_02120 | ||||||
Sites | |||||||||
| Binding site | 241 | 1 | Pyridoxal phosphate; via amide nitrogen By similarity HAMAP MF_02120 | ||||||
| Binding site | 281 | 1 | Substrate By similarity HAMAP MF_02120 | ||||||
| Binding site | 317 | 1 | Substrate By similarity HAMAP MF_02120 | ||||||
| Binding site | 321 | 1 | Substrate By similarity HAMAP MF_02120 | ||||||
| Binding site | 349 | 1 | Substrate By similarity HAMAP MF_02120 | ||||||
| Binding site | 376 | 1 | Pyridoxal phosphate By similarity HAMAP MF_02120 | ||||||
| Binding site | 376 | 1 | Substrate By similarity HAMAP MF_02120 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 62 | 1 | N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_02120 | ||||||
Sequences
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References
| [1] | "Structural flexibility in the Burkholderia mallei genome." Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004) [PubMed: 15377793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23344. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000010 Genomic DNA. Translation: AAU47904.1. |
| RefSeq | YP_104274.1. NC_006348.1. |
3D structure databases | |
| ProteinModelPortal | Q62GA0. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3091324. |
| GenomeReviews | Gene locus BMA2756 in contig CP000010_GR. |
| KEGG | bma:BMA2756. |
| PATRIC | 19120663. VBIBurMal55007_2825. |
| TIGR | BMA2756. |
Phylogenomic databases | |
| HOGENOM | HOG000045070. |
| KO | K01586. |
| OMA | DAHTHPY. |
| ProtClustDB | CLSK897530. |
Family and domain databases | |
| Gene3D | G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 1 hit. |
| HAMAP | MF_02120. LysA. [Tree] |
| InterPro | IPR009006. Ala_racemase/Decarboxylase_C. IPR002986. DAP_deCOOHase_LysA. IPR022643. De-COase2_C. IPR022657. De-COase2_CS. IPR022644. De-COase2_N. IPR000183. Orn/DAP/Arg_de-COase. [Graphical view] |
| Pfam | PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view] |
| PRINTS | PR01181. DAPDCRBXLASE. PR01179. ODADCRBXLASE. |
| SUPFAM | SSF50621. Racem_decarbox_C. 1 hit. |
| TIGRFAMs | TIGR01048. LysA. 1 hit. |
| PROSITE | PS00879. ODR_DC_2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q62GA0_BURMA | ||||||||
| Accession | Primary (citable) accession number: Q62GA0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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