A9MU62 (DCYD_SALPB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 35.
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 | Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1016998 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
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_1000084408 | |||||
Amino acid modifications | |||||||||
| Modified residue | 51 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | The Salmonella enterica serovar Paratyphi B Genome Sequencing Project McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1250 / SPB7. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000886 Genomic DNA. Translation: ABX66618.1. |
| RefSeq | YP_001587451.1. NC_010102.1. |
3D structure databases | |
| ProteinModelPortal | A9MU62. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272994.SPAB_01203. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABX66618; ABX66618; SPAB_01203. |
| GeneID | 5783082. |
| KEGG | spq:SPAB_01203. |
| PATRIC | 18530242. VBISalEnt120821_1000. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2515. |
| HOGENOM | HOG000022459. |
| KO | K05396. |
| OMA | PYLVPIG. |
| ProtClustDB | PRK03910. |
Enzyme and pathway databases | |
| BioCyc | SENT28901:GH9O-1201-MONOMER. |
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_SALPB | ||||||||
| Accession | Primary (citable) accession number: A9MU62 | ||||||||
| 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
