ID   3HYPE_BURM1             Reviewed;         335 AA.
AC   A9AKG8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=3-hydroxyproline 2-epimerase {ECO:0000303|PubMed:24980702};
DE            Short=3Hyp 2-epimerase;
DE            Short=3HypE {ECO:0000303|PubMed:24980702};
DE            EC=5.1.1.- {ECO:0000269|PubMed:24980702};
GN   Name=prdF {ECO:0000312|EMBL:BAG46103.1};
GN   OrderedLocusNames=Bmul_4260 {ECO:0000312|EMBL:ABX17941.1},
GN   BMULJ_04246 {ECO:0000312|EMBL:BAG46103.1};
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=24980702; DOI=10.7554/elife.03275;
RA   Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B.,
RA   San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A.,
RA   Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.;
RT   "Prediction and characterization of enzymatic activities guided by sequence
RT   similarity and genome neighborhood networks.";
RL   Elife 3:E03275-E03275(2014).
CC   -!- FUNCTION: Catalyzes the epimerization of trans-3-hydroxy-L-proline
CC       (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Can also
CC       catalyze the epimerization of trans-4-hydroxy-L-proline (t3LHyp) to
CC       cis-4-hydroxy-D-proline (c4DHyp), albeit with 3.6-fold lower
CC       efficiency. Displays no proline racemase activity.
CC       {ECO:0000269|PubMed:24980702}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=trans-3-hydroxy-L-proline = cis-3-hydroxy-D-proline;
CC         Xref=Rhea:RHEA:47712, ChEBI:CHEBI:57938, ChEBI:CHEBI:87840;
CC         Evidence={ECO:0000269|PubMed:24980702};
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         Evidence={ECO:0000269|PubMed:24980702};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.7 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         KM=18 mM for trans-3-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 1.3 sec(-1) for t4LHyp epimerization. kcat is 30 sec(-1)
CC         for t3LHyp epimerization. {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000869; ABX17941.1; -; Genomic_DNA.
DR   EMBL; AP009386; BAG46103.1; -; Genomic_DNA.
DR   RefSeq; WP_012217013.1; NC_010805.1.
DR   AlphaFoldDB; A9AKG8; -.
DR   SMR; A9AKG8; -.
DR   STRING; 395019.Bmul_4260; -.
DR   EnsemblBacteria; BAG46103; BAG46103; BMULJ_04246.
DR   KEGG; bmj:BMULJ_04246; -.
DR   KEGG; bmu:Bmul_4260; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_0_0_4; -.
DR   OMA; ERRAYCM; -.
DR   SABIO-RK; A9AKG8; -.
DR   Proteomes; UP000008815; Chromosome 2.
DR   GO; GO:0047580; F:4-hydroxyproline epimerase activity; IEA:RHEA.
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..335
FT                   /note="3-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432253"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         92..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         256..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   335 AA;  36485 MW;  969330844ABE0E76 CRC64;
     MKISRSLSTV EVHTGGEAFR IVTSGLPRLP GDTIVRRRAW LKEHADEIRR ALMFEPRGHA
     DMYGGYLTEP VSPNADFGVI FVHNEGYSDH CGHGVIALST AAVELGWVQR TVPETRVGID
     APCGFIEAFV QWDGEHAGPV RFVNVPSFIW QRDVAVDTPS FGTVTGDIAY GGAFYFYVDG
     APFDLPVRES AVERLIRFGA EVKAAANAKY PVEHPEIPEI NHIYGTIIAN APRDPRSTQA
     NCCVFADREV DRSPTGSGTG GRVAQLYQRG LLAAGDTLVN ESIVGTVFKG RVLRETTVGG
     MPAVIPEVEG SAHICGFANW IVDERDPLTY GFLVR