Q2KHU0 (SERB_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
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: Phosphoserine phosphatase Short name=PSP Short name=PSPase EC=3.1.3.3 Alternative name(s): L-3-phosphoserine phosphatase O-phosphoserine phosphohydrolase | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 225 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates By similarity. |
| Catalytic activity | O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Pathway | Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the serB family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Serine biosynthesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | L-serine biosynthetic process Inferred from sequence or structural similarity. Source: RefGenome |
| Cellular component | cytoplasm Inferred from sequence or structural similarity. Source: RefGenome |
| Molecular function | calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion bindingInferred from sequence or structural similarity. Source: UniProtKB phosphoserine phosphatase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 225 | 225 | Phosphoserine phosphatase | PRO_0000244407 | |||||
Regions | |||||||||
| Region | 109 – 110 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 20 | 1 | Nucleophile By similarity | ||||||
| Active site | 22 | 1 | Proton donor By similarity | ||||||
| Metal binding | 20 | 1 | Magnesium By similarity | ||||||
| Metal binding | 22 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 179 | 1 | Magnesium By similarity | ||||||
| Binding site | 29 | 1 | Substrate By similarity | ||||||
| Binding site | 65 | 1 | Substrate By similarity | ||||||
| Binding site | 158 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC112884 mRNA. Translation: AAI12885.1. |
| IPI | IPI00701167. |
| RefSeq | NP_001039820.1. NM_001046355.1. |
| UniGene | Bt.25099. |
3D structure databases | |
| ProteinModelPortal | Q2KHU0. |
| SMR | Q2KHU0. Positions 4-225. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2KHU0. |
Proteomic databases | |
| PRIDE | Q2KHU0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000017392; ENSBTAP00000017392; ENSBTAG00000013081. |
| GeneID | 533630. |
| KEGG | bta:533630. |
Organism-specific databases | |
| CTD | 5723. |
Phylogenomic databases | |
| eggNOG | maNOG12671. |
| GeneTree | ENSGT00390000003115. |
| HOVERGEN | HBG057486. |
| InParanoid | Q2KHU0. |
| OrthoDB | EOG4NVZM5. |
| PhylomeDB | Q2KHU0. |
Family and domain databases | |
| InterPro | IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. IPR006383. HAD-SF_hydro_IB_PSP-like. IPR023190. Pser_Pase_dom_2. IPR004469. SerB. [Graphical view] |
| Gene3D | G3DSA:3.40.50.1000. HAD-like_dom. 2 hits. G3DSA:1.10.150.210. Pser_Pase_dom_2. 1 hit. |
| KO | K01079. |
| Pfam | PF00702. Hydrolase. 1 hit. [Graphical view] |
| SUPFAM | SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR01488. HAD-SF-IB. 1 hit. TIGR00338. SerB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | SERB_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q2KHU0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with