P0ABK6 (CYSK_ECO57) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 48.
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 Sulfate starvation-induced protein 5 Short name=SSI5 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
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)
| 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_0000167087 | |||||
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] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG57533.1. BA000007 Genomic DNA. Translation: BAB36709.1. |
| PIR | A85884. F91039. |
| RefSeq | NP_288976.1. NC_002655.2. NP_311313.1. NC_002695.1. |
3D structure databases | |
| ProteinModelPortal | P0ABK6. |
| SMR | P0ABK6. Positions 2-305. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000028593; EBESCP00000027486; EBESCG00000027644. EBESCT00000056761; EBESCP00000054589; EBESCG00000055809. |
| GeneID | 915544. 957634. |
| GenomeReviews | Gene locus Z3680 in contig AE005174_GR. Gene locus ECs3286 in contig BA000007_GR. |
| KEGG | ece:Z3680. ecs:ECs3286. |
| PATRIC | 18355988. VBIEscCol44059_3189. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009701. |
| HOGENOM | HBG748215. |
| OMA | AHSIGNT. |
| ProtClustDB | PRK10717. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS3286-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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0ABK6 Secondary accession number(s): P11096, P21546 | ||||||||
| 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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