Q5XAQ3 (CYSK_STRP6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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 Short name=CSase EC=2.5.1.47 Alternative name(s): O-acetylserine (thiol)-lyase Short name=OAS-TL O-acetylserine sulfhydrylase | ||||
| Gene names |
| ||||
| Organism | Streptococcus pyogenes serotype M6 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 301450 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 313 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | O(3)-acetyl-L-serine + H2S = L-cysteine + acetate. |
| Cofactor | Pyridoxal phosphate By similarity. UniProtKB P47998 |
| Pathway | Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. UniProtKB P47998 |
| Subunit structure | Homodimer By similarity. UniProtKB P47998 |
| 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 | Complete proteome Direct protein sequencing |
| 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 Ref.2 | ||||||
| Chain | 2 – 313 | 312 | Cysteine synthase | PRO_0000259398 | |||||
Regions | |||||||||
| Region | 179 – 183 | 5 | Pyridoxal phosphate binding By similarity UniProtKB P47998 | ||||||
| Region | 215 – 220 | 6 | SAT1 binding By similarity UniProtKB P47998 | ||||||
Sites | |||||||||
| Binding site | 75 | 1 | Pyridoxal phosphate By similarity UniProtKB P47998 | ||||||
| Binding site | 267 | 1 | Pyridoxal phosphate By similarity UniProtKB P47998 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 45 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain." Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M. J. Infect. Dis. 190:727-738(2004) [PubMed: 15272401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-946 / MGAS10394 / Serotype M6. |
| [2] | "Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins." Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A. Submitted (MAY-2000) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-22; 91-124 AND 221-243. Strain: JRS4 / Serotype M6. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000003 Genomic DNA. Translation: AAT87510.1. |
| RefSeq | YP_060693.1. NC_006086.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1Z7W based on UniProtKB P47998. |
| ProteinModelPortal | Q5XAQ3. |
| SMR | Q5XAQ3. Positions 1-307. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTRT00000038858; EBSTRP00000037431; EBSTRG00000038856. |
| GeneID | 2942124. |
| GenomeReviews | Gene locus M6_Spy1375 in contig CP000003_GR. |
| KEGG | spa:M6_Spy1375. |
| PATRIC | 19724991. VBIStrPyo30273_1428. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000028105. |
| HOGENOM | HBG748215. |
| OMA | RRNMIKA. |
| ProtClustDB | CLSK698791. |
Enzyme and pathway databases | |
| BioCyc | SPYO286636:M6_SPY1375-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_STRP6 | ||||||||
| Accession | Primary (citable) accession number: Q5XAQ3 Secondary accession number(s): P82484 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with