Q8FYS0 (HYPRE_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
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: 4-hydroxyproline epimerase EC=5.1.1.8 Alternative name(s): Hydroxyproline-2-epimerase Short name=BsHyPRE | ||
| Gene names |
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| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 204722 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › ![]() |
Protein attributes
| Sequence length | 333 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting 4-hydroxy-L-proline to 4-hydroxy-D-proline, which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways. |
| Catalytic activity | Trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline. Ref.1 |
| Enzyme regulation | Inhibited by iodoacetate, iodoacetamide and by high amounts (10mM) of pyrrole-2-carboxylic acid (PYC). Not inhibited by PYC at 1mM. Ref.1 |
| Subunit structure | Homodimer By similarity. |
| Miscellaneous | This enzyme does not require pyridoxal phosphate (PLP) as a cofactor. |
| Sequence similarities | Belongs to the proline racemase family. 4-hydroxyproline epimerase subfamily. |
| Biophysicochemical properties | Kinetic parameters: KM=7.6 mM for 4-hydroxy-L-proline Ref.1 KM=10.8 mM for 4-hydroxy-D-proline Vmax=0.50 µM/sec/mg enzyme with L-proline as substrate (at 37 degrees Celsius) Vmax=0.75 µM/sec/mg enzyme with D-proline as substrate (at 37 degrees Celsius) |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular_function | 4-hydroxyproline epimerase activity Inferred from electronic annotation. Source: EC proline racemase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular and structural discrimination of proline racemase and hydroxyproline-2-epimerase from nosocomial and bacterial pathogens." Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A., Minoprio P. PLoS ONE 2:E885-E885(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 1330. |
| [2] | "The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [3] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EF495343 Genomic DNA. Translation: ABS82395.1. AE014291 Genomic DNA. Translation: AAN30688.1. CP002997 Genomic DNA. Translation: AEM19105.1. |
| RefSeq | NP_698773.1. NC_004310.3. YP_005616597.1. NC_017251.1. |
3D structure databases | |
| ProteinModelPortal | Q8FYS0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 204722.BR1792. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN30688; AAN30688; BR1792. AEM19105; AEM19105; BS1330_I1786. |
| GeneID | 1167485. 12137556. |
| KEGG | bms:BR1792. bsi:BS1330_I1786. |
| PATRIC | 17791972. VBIBruSui107850_1819. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3938. |
| HOGENOM | HOG000084336. |
| KO | K12658. |
| OMA | CNIPAFL. |
| ProtClustDB | PRK13971. |
Enzyme and pathway databases | |
| BRENDA | 5.1.1.8. 8693. |
Family and domain databases | |
| InterPro | IPR008794. Pro_racemase. [Graphical view] |
| Pfam | PF05544. Pro_racemase. 1 hit. [Graphical view] |
| PIRSF | PIRSF029792. Pro_racemase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HYPRE_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FYS0 Secondary accession number(s): A8DEY2, G0K7C9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
