ID   4HPE2_BURM1             Reviewed;         338 AA.
AC   A9AQW9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=4-hydroxyproline 2-epimerase 2 {ECO:0000303|PubMed:24980702};
DE            Short=4Hyp 2-epimerase 2;
DE            Short=4HypE 2 {ECO:0000303|PubMed:24980702};
DE            EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN   Name=prdF {ECO:0000312|EMBL:BAG45129.1};
GN   OrderedLocusNames=Bmul_5265 {ECO:0000312|EMBL:ABX18935.1},
GN   BMULJ_03255 {ECO:0000312|EMBL:BAG45129.1};
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-4-hydroxy-L-proline
CC       (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a
CC       degradation pathway that converts t4LHyp to alpha-ketoglutarate.
CC       Displays no proline racemase activity. {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         EC=5.1.1.8; Evidence={ECO:0000269|PubMed:24980702};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11 mM for trans-4-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 5.6 sec(-1) for trans-4-hydroxy-L-proline epimerization.
CC         kcat is 0.34 sec(-1) for trans-3-hydroxy-L-proline epimerization.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000869; ABX18935.1; -; Genomic_DNA.
DR   EMBL; AP009386; BAG45129.1; -; Genomic_DNA.
DR   RefSeq; WP_012217743.1; NC_010805.1.
DR   AlphaFoldDB; A9AQW9; -.
DR   SMR; A9AQW9; -.
DR   STRING; 395019.Bmul_5265; -.
DR   EnsemblBacteria; BAG45129; BAG45129; BMULJ_03255.
DR   KEGG; bmj:BMULJ_03255; -.
DR   KEGG; bmu:Bmul_5265; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_0_0_4; -.
DR   OMA; SHVLWTG; -.
DR   SABIO-RK; A9AQW9; -.
DR   Proteomes; UP000008815; Chromosome 2.
DR   GO; GO:0047580; F:4-hydroxyproline epimerase activity; IDA:CACAO.
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..338
FT                   /note="4-hydroxyproline 2-epimerase 2"
FT                   /id="PRO_0000432276"
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         223
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   338 AA;  36866 MW;  F2295223816715C5 CRC64;
     MTIHGFTCIE GHTEGMPVRM VIDGAPTLQG ATMNARREDF VAHHDWVRRT LMLEPRGHAH
     MSGTIFYPPV SDNADFSLLF IETSGCLPMC GHATIGSIAF AIEERLVVPK RPGTVTVDVP
     AGQIVARYQT DGERVTSVRF TNVPSFLLKR DVEIAIPALG TLAVDIAYGG NFYPIVEVQP
     NFPGCEHFTP DELLAWGRDV QRAVGDALEV VHPDNPAIRG VRHCMWTGKP IADDAHGRAV
     VIAGDSLVDR SPCGTGSSAR VAQRFARGWL KEGEAYCHES LIGSRFIGRV ESTVRLESGV
     DAVLSSIEGR AWVTGRAQYR VDPSQPYALG FSLQEFVN