Reviewed,
UniProtKB/Swiss-Prot Q1R2Q6 (SDHD2_ECOUT)
Last modified
June 16, 2009.
Version 21.
History...
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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: D-serine dehydratase 2 EC=4.3.1.18 Alternative name(s): D-serine deaminase 2 Short name=DSD 2 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 364106 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 442 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. |
| Subunit structure | Monomer 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 – 442 | 442 | D-serine dehydratase 2 HAMAP MF_01030 | PRO_0000291727 | |||||
Amino acid modifications | |||||||||
| Modified residue | 118 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000243 Genomic DNA. Translation: ABE10358.1. | |
| RefSeq | YP_543889.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3990843. |
| GenomeReviews | Gene locus UTI89_C4955 in contig CP000243_GR. |
| KEGG | eci:UTI89_C4955. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q1R2Q6. |
| OMA | Q1R2Q6. DHPLFVY. |
Enzyme and pathway databases | |
| BioCyc | ECOL364106:UTI89_C4955-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 | SDHD2_ECOUT | ||||||||
| Accession | Primary (citable) accession number: Q1R2Q6 | ||||||||
| 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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