Reviewed,
UniProtKB/Swiss-Prot P16095 (SDHL_ECOLI)
Last modified
November 3, 2009.
Version 81.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-serine dehydratase 1 Short name=SDH 1 EC=4.3.1.17 Alternative name(s): L-serine deaminase 1 Short name=L-SD1 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 454 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Deaminates also threonine, particularly when it is present in high concentration. |
| Catalytic activity | L-serine = pyruvate + NH3. |
| Cofactor | Binds 1 4Fe-4S cluster Probable. |
| Pathway | |
| Induction | It is made aerobically and anaerobically, in minimal medium. |
| Post-translational modification | Activated by post-translational modification by a system involving at least three gene products. Activation is mimicked in vitro by iron and dithiothreitol. There is considerable evidence for a free-radical activation mechanism. |
| Sequence similarities | Belongs to the iron-sulfur dependent L-serine dehydratase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | gluconeogenesis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW L-serine ammonia-lyase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 454 | 454 | L-serine dehydratase 1 | PRO_0000171903 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "L-serine degradation in Escherichia coli K-12: cloning and sequencing of the sdaA gene." Su H., Lang B.F., Newman E.B. J. Bacteriol. 171:5095-5102(1989) [PubMed: 2504697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Use of gene fusions of the structural gene sdaA to purify L-serine deaminase 1 from Escherichia coli K-12." Su H., Moniakis J., Newman E.B. Eur. J. Biochem. 211:521-527(1993) [PubMed: 8436113] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION, CHARACTERIZATION. Strain: K12. |
| [3] | "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. Horiuchi T.DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
Cross-references
Sequence databases | |
|---|---|
| M28695 Genomic DNA. Translation: AAA63580.1. U00096 Genomic DNA. Translation: AAC74884.1. AP009048 Genomic DNA. Translation: BAA15621.1. | |
| PIR | DWECL. F64942. |
| RefSeq | AP_002433.1. NP_416328.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P16095. |
Genome annotation databases | |
| GeneID | 946331. |
| GenomeReviews | Gene locus JW1803 in contig AP009048_GR. Gene locus b1814 in contig U00096_GR. |
| KEGG | ecj:JW1803. eco:b1814. |
Organism-specific databases | |
| EchoBASE | EB0923. |
| EcoGene | EG10930. sdaA. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P16095. |
| OMA | ENANELQ. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:LSERINEDEAM1-MON. MetaCyc:LSERINEDEAM1-MON. |
Gene expression databases | |
| Genevestigator | P16095. |
Family and domain databases | |
| InterPro | IPR004644. Fe-S_L-Ser_mono. IPR005130. Ser_deHydtase_asu. IPR005131. Ser_deHydtase_bsu. [Graphical view] |
| Pfam | PF03313. SDH_alpha. 1 hit. PF03315. SDH_beta. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00720. sda_mono. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | SDHL_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P16095 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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