B7MY25 (SDHD_ECO81) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 29.
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-serine dehydratase EC=4.3.1.18 Alternative name(s): D-serine deaminase Short name=DSD | ||||
| Gene names |
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| Organism | Escherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 585397 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 442 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | D-serine = pyruvate + NH3. HAMAP-Rule MF_01030 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP-Rule MF_01030 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_01030 |
| Sequence similarities | Belongs to the serine/threonine dehydratase family. DsdA subfamily. |
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-serine ammonia-lyase activity Inferred from electronic annotation. Source: EC hydro-lyase activityInferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 442 | 442 | D-serine dehydratase HAMAP-Rule MF_01030 | PRO_1000149388 | |||||
Amino acid modifications | |||||||||
| Modified residue | 118 | 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: ED1a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU928162 Genomic DNA. Translation: CAR08991.2. |
| RefSeq | YP_002398721.1. NC_011745.1. |
3D structure databases | |
| ProteinModelPortal | B7MY25. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAR08991; CAR08991; ECED1_2813. |
| GeneID | 7140527. |
| KEGG | ecq:ECED1_2813. |
| PATRIC | 38489650. VBIEscCol8292_2818. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3048. |
| HOGENOM | HOG000218072. |
| KO | K01753. |
| OMA | HCLFAEP. |
| ProtClustDB | PRK02991. |
Enzyme and pathway databases | |
| BioCyc | ECOL585397:GJCU-2845-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01030. D-Ser_dehydrat. |
| InterPro | IPR011780. D_Ser_am_lyase. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view] |
| PANTHER | PTHR10314:SF9. PTHR10314:SF9. 1 hit. |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| SUPFAM | SSF53686. PyrdxlP-dep_enz_bsu. 1 hit. |
| TIGRFAMs | TIGR02035. D_Ser_am_lyase. 1 hit. |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SDHD_ECO81 | ||||||||
| Accession | Primary (citable) accession number: B7MY25 | ||||||||
| 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
