ID   4HYPE_BURPB             Reviewed;         320 AA.
AC   C5ZMD2;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=4-hydroxyproline 2-epimerase {ECO:0000303|PubMed:24980702};
DE            Short=4Hyp 2-epimerase;
DE            Short=4HypE {ECO:0000303|PubMed:24980702};
DE            EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN   ORFNames=BURPS1106B_1521 {ECO:0000312|EMBL:EES20685.1};
OS   Burkholderia pseudomallei (strain 1106b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357347;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106b;
RA   Harkins D.M., DeShazer D., Woods D.E., Brinkac L.M., Brown K.A., Hung G.C.,
RA   Tuanyok A., Zhang B., Nierman W.C.;
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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       {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   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CM000775; EES20685.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5ZMD2; -.
DR   SMR; C5ZMD2; -.
DR   HOGENOM; CLU_036729_1_0_4; -.
DR   Proteomes; UP000007034; Chromosome II.
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..320
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432287"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        246
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         99..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         247..248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   320 AA;  33363 MW;  4365AF6F0196E6F2 CRC64;
     MRISTLDRRD 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