Q00834 (CYSK_SPIOL) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 78.
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 EC=2.5.1.47 Alternative name(s): CSase A O-acetylserine (thiol)-lyase Short name=OAS-TL A O-acetylserine sulfhydrylase |
| Organism | Spinacia oleracea (Spinach) |
| Taxonomic identifier | 3562 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia![]() |
Protein attributes
| Sequence length | 325 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | O(3)-acetyl-L-serine + H2S = L-cysteine + acetate. |
| Cofactor | Pyridoxal phosphate. |
| Pathway | Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 2/2. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Leaves and roots. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the cysteine synthase/cystathionine beta-synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Cysteine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | cysteine synthase activity Inferred from electronic annotation. Source: EC 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 325 | 325 | Cysteine synthase | PRO_0000167125 | |||||
Regions | |||||||||
| Region | 184 – 188 | 5 | Pyridoxal phosphate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 80 | 1 | Pyridoxal phosphate By similarity | ||||||
| Binding site | 272 | 1 | Pyridoxal phosphate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 49 | 1 | N6-(pyridoxal phosphate)lysine | ||||||
Sequences
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References
| [1] | "Molecular cloning and bacterial expression of cDNA encoding a plant cysteine synthase." Saito K., Miura N., Yamazaki M., Hirano H., Murakoshi I. Proc. Natl. Acad. Sci. U.S.A. 89:8078-8082(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-11; 71-90; 163-182 AND 246-262. Strain: cv. Parade. Tissue: Leaf. |
| [2] | "Determination of a functional lysine residue of a plant cysteine synthase by site-directed mutagenesis, and the molecular evolutionary implications." Saito K., Kurosawa M., Murakoshi I. FEBS Lett. 328:111-114(1993) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYSINE RESIDUES. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D10476 mRNA. Translation: BAA01279.1. |
| PIR | S35094. |
3D structure databases | |
| ProteinModelPortal | Q00834. |
| SMR | Q00834. Positions 8-325. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00136; UER00200. |
Family and domain databases | |
| InterPro | IPR001216. Cys_synth_BS. IPR005856. Cys_synthKM. IPR005859. CysK. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view] |
| 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_SPIOL | ||||||||
| Accession | Primary (citable) accession number: Q00834 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
