ID   4HYPE_BRUAB             Reviewed;         333 AA.
AC   Q57B94; A8DEY8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=4-hydroxyproline epimerase;
DE            EC=5.1.1.8;
DE   AltName: Full=Hydroxyproline-2-epimerase;
DE            Short=BaHyPRE;
GN   OrderedLocusNames=BruAb1_1773;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ROLE IN VIRULENCE.
RC   STRAIN=544 / Biovar 1;
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=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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. Strong B-cell mitogen.
CC       Plays an important role in the regulation of intra- and extracellular
CC       amino acid pools, allowing the bacterium to profit from host precursors
CC       and enzymatic pathways. {ECO:0000269|PubMed:17849014}.
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=9.8 mM for 4-hydroxy-L-proline {ECO:0000269|PubMed:17849014};
CC         KM=10.8 mM for 4-hydroxy-D-proline {ECO:0000269|PubMed:17849014};
CC         Vmax=0.40 uM/sec/mg enzyme with L-proline as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:17849014};
CC         Vmax=0.75 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; EF495344; ABS82396.1; -; Genomic_DNA.
DR   EMBL; AE017223; AAX75090.1; -; Genomic_DNA.
DR   RefSeq; WP_002964871.1; NC_006932.1.
DR   AlphaFoldDB; Q57B94; -.
DR   SMR; Q57B94; -.
DR   EnsemblBacteria; AAX75090; AAX75090; BruAb1_1773.
DR   GeneID; 3788305; -.
DR   KEGG; bmb:BruAb1_1773; -.
DR   HOGENOM; CLU_036729_0_0_5; -.
DR   OMA; SHVLWTG; -.
DR   BRENDA; 5.1.1.8; 994.
DR   Proteomes; UP000000540; Chromosome I.
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.
FT   CHAIN           1..333
FT                   /note="4-hydroxyproline epimerase"
FT                   /id="PRO_0000354027"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        253
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         91..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   333 AA;  36670 MW;  34DA2AA5674D5FB9 CRC64;
     MARHSFFCVD GHTCGNPVRL VAGGGPNLNG STMMEKRAHF LAEYDWIRTG LMFEPRGHDM
     MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTVTM AIEQGLVTPK TPGKLNLDTP
     AGLVAIEYEQ DGQYVERVRL TNVPAFLYAE GLEVECPDLG PIKVDVAYGG NFYAIVEPQE
     NYTDMDDYSA LQLIAWSPVL RQRLNEKYKF QHPELPDINR LSHILWTGKP KHPQAHARNA
     VFYGDKAIDR SPCGTGTSAR MAQLAAKGKL KPCDEFIHES IIGSLFHGRV ERAAEVAGRP
     AIVPSIAGWA RMTGYNTIFI DDRDPFAHGF SMA