Reviewed,
UniProtKB/Swiss-Prot Q0I5V1 (SDHD_HAES1)
Last modified
June 16, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Probable D-serine dehydratase EC=4.3.1.18 Alternative name(s): D-serine deaminase Short name=DSD | ||||
| Gene names |
| ||||
| Organism | Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 205914 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus |
Protein attributes
| Sequence length | 438 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | D-serine = pyruvate + NH3. HAMAP MF_01030 |
| Cofactor | Pyridoxal phosphate By similarity. |
| 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 – 438 | 438 | Probable D-serine dehydratase HAMAP MF_01030 | PRO_0000291732 | |||||
Amino acid modifications | |||||||||
| Modified residue | 114 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd." Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J. J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000436 Genomic DNA. Translation: ABI25986.1. Different initiation. | |
| RefSeq | YP_719923.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4241250. |
| GenomeReviews | Gene locus HS_1718 in contig CP000436_GR. |
| KEGG | hso:HS_1718. |
| NMPDR | fig|205914.1.peg.1659. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q0I5V1. |
Enzyme and pathway databases | |
| BioCyc | HSOM205914:HS_1718-MON. |
Family and domain databases | |
| HAMAP | MF_01030. [Tree] |
| InterPro | IPR011780. D_Ser_am_lyase. IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. [Graphical view] |
| PANTHER | PTHR10314:SF9. D_Ser_am_lyase. 1 hit. |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02035. D_Ser_am_lyase. 1 hit. |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SDHD_HAES1 | ||||||||
| Accession | Primary (citable) accession number: Q0I5V1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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