P0A1E4 (CYSK_SALTI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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: Cysteine synthase A Short name=CSase A EC=2.5.1.47 Alternative name(s): O-acetylserine (thiol)-lyase A Short name=OAS-TL A O-acetylserine sulfhydrylase A | ||||
| Gene names |
| ||||
| Organism | Salmonella typhi [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90370 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 323 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product By similarity. |
| Catalytic activity | O(3)-acetyl-L-serine + H2S = L-cysteine + acetate. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the cysteine synthase/cystathionine beta-synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Cysteine biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Transferase |
| Technical term | Allosteric enzyme Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro |
| Molecular function | cysteine synthase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro transferase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 323 | 322 | Cysteine synthase A | PRO_0000167088 | |||||
Regions | |||||||||
| Region | 177 – 181 | 5 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 8 | 1 | Allosteric inhibitor By similarity | ||||||
| Binding site | 72 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 269 | 1 | Allosteric inhibitor; via amide nitrogen By similarity | ||||||
| Binding site | 273 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 42 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18." Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. Barrell B.G.Nature 413:848-852(2001) [PubMed: 11677608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT18. |
| [2] | "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18." Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R. J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700931 / Ty2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL627274 Genomic DNA. Translation: CAD07662.1. AE014613 Genomic DNA. Translation: AAO68145.1. |
| RefSeq | NP_456967.1. NC_003198.1. NP_804296.1. NC_004631.1. |
3D structure databases | |
| ProteinModelPortal | P0A1E4. |
| SMR | P0A1E4. Positions 2-323. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0A1E4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1068474. 1248985. |
| GenomeReviews | Gene locus t0427 in contig AE014613_GR. Gene locus STY2666 in contig AL513382_GR. |
| KEGG | stt:t0427. sty:STY2666. |
| PATRIC | 18543322. VBISalEnt120419_2702. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG748215. |
| OMA | AHSIGNT. |
| ProtClustDB | PRK10717. |
Enzyme and pathway databases | |
| BioCyc | SENT209261:T0427-MONOMER. SENT220341:STY2666-MONOMER. |
Family and domain databases | |
| InterPro | IPR001216. Cys_synth_BS. IPR005856. Cys_synthKM. IPR005859. CysK. IPR001926. PyrdxlP-dep_enz_bsu. [Graphical view] |
| KO | K01738. |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| SUPFAM | SSF53686. PyrdxlP-dep_enz_bsu. 1 hit. |
| TIGRFAMs | TIGR01139. CysK. 1 hit. TIGR01136. CysKM. 1 hit. |
| PROSITE | PS00901. CYS_SYNTHASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYSK_SALTI | ||||||||
| Accession | Primary (citable) accession number: P0A1E4 Secondary accession number(s): P12674 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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