B7NBR4 (DCYD_ECOLU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 32.
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: D-cysteine desulfhydrase EC=4.4.1.15 | ||||
| Gene names |
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| Organism | Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 585056 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 328 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine By similarity. HAMAP-Rule MF_01045 |
| Catalytic activity | D-cysteine + H2O = H2S + NH3 + pyruvate. HAMAP-Rule MF_01045 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the ACC deaminase/D-cysteine desulfhydrase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | D-amino acid metabolic process Inferred from electronic annotation. Source: HAMAP |
| Molecular_function | D-cysteine desulfhydrase activity Inferred 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 – 328 | 328 | D-cysteine desulfhydrase HAMAP-Rule MF_01045 | PRO_1000136161 | |||||
Amino acid modifications | |||||||||
| Modified residue | 51 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. Denamur E.PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UMN026 / ExPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU928163 Genomic DNA. Translation: CAR13404.1. |
| RefSeq | YP_002412933.1. NC_011751.1. |
3D structure databases | |
| ProteinModelPortal | B7NBR4. |
| SMR | B7NBR4. Positions 4-328. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 585056.ECUMN_2211. |
Proteomic databases | |
| PRIDE | B7NBR4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAR13404; CAR13404; ECUMN_2211. |
| GeneID | 7158785. |
| KEGG | eum:ECUMN_2211. |
| PATRIC | 18443683. VBIEscCol32010_2400. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2515. |
| HOGENOM | HOG000022459. |
| KO | K05396. |
| OMA | PYLVPIG. |
| ProtClustDB | PRK03910. |
Family and domain databases | |
| HAMAP | MF_01045. D-Cys_desulfhydr. |
| InterPro | IPR027278. ACCD_DCysDesulf. IPR005966. D-Cys_desShydrase. IPR023702. D_Cys_desulphydr_bac. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| PIRSF | PIRSF006278. ACCD_DCysDesulf. 1 hit. |
| SUPFAM | SSF53686. PyrdxlP-dep_enz_bsu. 1 hit. |
| TIGRFAMs | TIGR01275. ACC_deam_rel. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DCYD_ECOLU | ||||||||
| Accession | Primary (citable) accession number: B7NBR4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
