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   27-MAR-2024, entry version 86.
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; Pseudomonadota; 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   GeneID; 56531207; -.
DR   KEGG; bps:BPSS0332; -.
DR   PATRIC; fig|272560.51.peg.6451; -.
DR   eggNOG; COG3938; Bacteria.
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; TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE; 1.
DR   PANTHER; PTHR33442:SF1; TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE; 1.
DR   Pfam; PF05544; Pro_racemase; 1.
DR   PIRSF; PIRSF029792; Pro_racemase; 1.
DR   SFLD; SFLDS00028; Proline_Racemase; 1.
DR   SUPFAM; SSF54506; Diaminopimelate epimerase-like; 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
//