4HYPE_BURPS
ID 4HYPE_BURPS Reviewed; 310 AA.
AC Q63NG7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=4-hydroxyproline epimerase;
DE EC=5.1.1.8;
DE AltName: Full=Hydroxyproline-2-epimerase;
DE Short=BpHyPRE;
GN OrderedLocusNames=BPSS0332;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K96243;
RX PubMed=17849014; DOI=10.1371/journal.pone.0000885;
RA Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A.,
RA Minoprio P.;
RT "Molecular and structural discrimination of proline racemase and
RT hydroxyproline-2-epimerase from nosocomial and bacterial pathogens.";
RL PLoS ONE 2:E885-E885(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- FUNCTION: Allows intracellular utilization of 4-hydroxyproline, one of
CC the major constituents of host collagen, by converting 4-hydroxy-L-
CC proline to 4-hydroxy-D-proline, which can be further metabolized by
CC intracellular 4-hydroxy-D-proline oxidases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline;
CC Xref=Rhea:RHEA:21152, ChEBI:CHEBI:57690, ChEBI:CHEBI:58375;
CC EC=5.1.1.8; Evidence={ECO:0000269|PubMed:17849014};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetate, iodoacetamide and by
CC high amounts (10 mM) of pyrrole-2-carboxylic acid (PYC). Not inhibited
CC by PYC at 1 mM. {ECO:0000269|PubMed:17849014}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.4 mM for 4-hydroxy-L-proline {ECO:0000269|PubMed:17849014};
CC KM=17.1 mM for 4-hydroxy-D-proline {ECO:0000269|PubMed:17849014};
CC Vmax=2.1 uM/sec/mg enzyme with L-proline as substrate (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:17849014};
CC Vmax=2.4 uM/sec/mg enzyme with D-proline as substrate (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:17849014};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: This enzyme does not require pyridoxal phosphate (PLP)
CC as a cofactor.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; EF495345; ABS82397.1; -; Genomic_DNA.
DR EMBL; BX571966; CAH37780.1; -; Genomic_DNA.
DR RefSeq; WP_004523447.1; NZ_CP009537.1.
DR RefSeq; YP_110352.1; NC_006351.1.
DR AlphaFoldDB; Q63NG7; -.
DR SMR; Q63NG7; -.
DR STRING; 272560.BPSS0332; -.
DR EnsemblBacteria; CAH37780; CAH37780; BPSS0332.
DR GeneID; 56531207; -.
DR KEGG; bps:BPSS0332; -.
DR PATRIC; fig|272560.51.peg.6451; -.
DR eggNOG; COG3938; Bacteria.
DR OMA; SHVLWTG; -.
DR BRENDA; 5.1.1.8; 1031.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0047580; F:4-hydroxyproline epimerase activity; IEA:UniProtKB-EC.
DR InterPro; IPR008794; Pro_racemase_fam.
DR PANTHER; PTHR33442; PTHR33442; 1.
DR Pfam; PF05544; Pro_racemase; 1.
DR PIRSF; PIRSF029792; Pro_racemase; 1.
DR SFLD; SFLDS00028; Proline_Racemase; 1.
PE 1: Evidence at protein level;
KW Isomerase; Reference proteome.
FT CHAIN 1..310
FT /note="4-hydroxyproline epimerase"
FT /id="PRO_0000354034"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 310 AA; 32118 MW; 4315A2A48443A002 CRC64;
MKHIHIIDSH TGGEPTRVVV SGFPALGGGT MAERLAVLAR EHDRYRAACI LEPRGSDVLV
GALLCEPVSA GAAAGVIFFN NAGYLGMCGH GTIGLVRTLH HMGRIGPGVH RIETPVGDVE
ATLHDDLSVS VRNVLAYRHA KDVVVDVPGH GAVTGDVAWG GNWFFLVSDH GQRVAGENVA
ALAAYASAVR AALERAGVTG RDGAPIDHIE LFADDPEYDS RSFVLCPGHA YDRSPCGTGT
SAKLACLAAD GKLAAGVTWR QASVIGSVFS ASYAAAEGGV VPTIRGSAHL SAEATLVIED
DDPFGWGIAS
