Q57B94 (HYPRE_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxyproline epimerase
EC=5.1.1.8

Alternative name(s):
Hydroxyproline-2-epimerase
Short name=BaHyPRE

Gene names

Ordered Locus Names:

BruAb1_1773

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

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. Ref.1
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=9.8 mM for 4-hydroxy-L-proline Ref.1 KM=10.8 mM for 4-hydroxy-D-proline Vmax=0.40 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 activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	4-hydroxyproline epimerase		PRO_0000354027
Sites
	Active site	90	1	Proton acceptor By similarity
	Active site	253	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57B94 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 34DA2AA5674D5FB9	FASTA	333	36,670
	10 20 30 40 50 60 MARHSFFCVD GHTCGNPVRL VAGGGPNLNG STMMEKRAHF LAEYDWIRTG LMFEPRGHDM 70 80 90 100 110 120 MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTVTM AIEQGLVTPK TPGKLNLDTP 130 140 150 160 170 180 AGLVAIEYEQ DGQYVERVRL TNVPAFLYAE GLEVECPDLG PIKVDVAYGG NFYAIVEPQE 190 200 210 220 230 240 NYTDMDDYSA LQLIAWSPVL RQRLNEKYKF QHPELPDINR LSHILWTGKP KHPQAHARNA 250 260 270 280 290 300 VFYGDKAIDR SPCGTGTSAR MAQLAAKGKL KPCDEFIHES IIGSLFHGRV ERAAEVAGRP 310 320 330 AIVPSIAGWA RMTGYNTIFI DDRDPFAHGF SMA

References

	« Hide 'large scale' referencesShow '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, ROLE IN VIRULENCE. Strain: 544 / Biovar 1.
[2]	"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF495344 Genomic DNA. Translation: ABS82396.1. AE017223 Genomic DNA. Translation: AAX75090.1.
RefSeq	YP_222451.1. NC_006932.1.
3D structure databases
HSSP	HSSP built from PDB template 1W61 based on UniProtKB Q4DA80.
ProteinModelPortal	Q57B94.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_1773.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX75090; AAX75090; BruAb1_1773.
GeneID	3340991.
KEGG	bmb:BruAb1_1773.
PATRIC	17825335. VBIBruAbo15061_1869.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3938.
HOGENOM	HOG000084336.
KO	K12658.
OMA	CNIPAFL.
ProtClustDB	PRK13971.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-1813-MONOMER.
BRENDA	5.1.1.8. 994.
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_BRUAB

Accession

Primary (citable) accession number: Q57B94
Secondary accession number(s): A8DEY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program