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Q63NG7 (HYPRE_BURPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxyproline epimerase

EC=5.1.1.8
Alternative name(s):
Hydroxyproline-2-epimerase
Short name=BpHyPRE
Gene names
Ordered Locus Names:BPSS0332
OrganismBurkholderia pseudomallei (strain K96243) [Reference proteome] [HAMAP]
Taxonomic identifier272560 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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=14.4 mM for 4-hydroxy-L-proline Ref.1

KM=17.1 mM for 4-hydroxy-D-proline

Vmax=2.1 µM/sec/mg enzyme with L-proline as substrate (at 37 degrees Celsius)

Vmax=2.4 µM/sec/mg enzyme with D-proline as substrate (at 37 degrees Celsius)

Ontologies

Keywords
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_function4-hydroxyproline epimerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

proline racemase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3103104-hydroxyproline epimerase
PRO_0000354034

Sites

Active site881Proton acceptor By similarity
Active site2361Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63NG7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 4315A2A48443A002

FASTA31032,118
        10         20         30         40         50         60 
MKHIHIIDSH TGGEPTRVVV SGFPALGGGT MAERLAVLAR EHDRYRAACI LEPRGSDVLV 

        70         80         90        100        110        120 
GALLCEPVSA GAAAGVIFFN NAGYLGMCGH GTIGLVRTLH HMGRIGPGVH RIETPVGDVE 

       130        140        150        160        170        180 
ATLHDDLSVS VRNVLAYRHA KDVVVDVPGH GAVTGDVAWG GNWFFLVSDH GQRVAGENVA 

       190        200        210        220        230        240 
ALAAYASAVR AALERAGVTG RDGAPIDHIE LFADDPEYDS RSFVLCPGHA YDRSPCGTGT 

       250        260        270        280        290        300 
SAKLACLAAD GKLAAGVTWR QASVIGSVFS ASYAAAEGGV VPTIRGSAHL SAEATLVIED 

       310 
DDPFGWGIAS 

« Hide

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: K96243.
[2]"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei."
Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. expand/collapse author list , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.
Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K96243.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF495345 Genomic DNA. Translation: ABS82397.1.
BX571966 Genomic DNA. Translation: CAH37780.1.
RefSeqYP_110352.1. NC_006351.1.

3D structure databases

ProteinModelPortalQ63NG7.
SMRQ63NG7. Positions 1-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272560.BPSS0332.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH37780; CAH37780; BPSS0332.
GeneID3097013.
KEGGbps:BPSS0332.
PATRIC19268294. VBIBurPse99623_4324.

Phylogenomic databases

eggNOGCOG3938.
HOGENOMHOG000084335.
KOK12658.
OMAWIRQALM.
OrthoDBEOG6SNDV3.

Enzyme and pathway databases

BioCycBPSE272560:GJNI-3867-MONOMER.
BRENDA5.1.1.8. 1031.

Family and domain databases

InterProIPR008794. Pro_racemase_fam.
[Graphical view]
PfamPF05544. Pro_racemase. 1 hit.
[Graphical view]
PIRSFPIRSF029792. Pro_racemase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHYPRE_BURPS
AccessionPrimary (citable) accession number: Q63NG7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families