ID   4HYPE_RHIEC             Reviewed;         345 AA.
AC   Q2KD13;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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   OrderedLocusNames=RHE_CH00452 {ECO:0000312|EMBL:ABC89273.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN   [2]
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). May be involved in a
CC       degradation pathway of t4LHyp. Can also catalyze the epimerization of
CC       trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp)
CC       in vitro, albeit with 2-fold lower efficiency. Displays no proline
CC       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=2.1 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         KM=2.1 mM for trans-3-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 1.9 sec(-1) for t4LHyp epimerization. kcat is 0.94 sec(-
CC         1) for t3LHyp epimerization. {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000133; ABC89273.1; -; Genomic_DNA.
DR   RefSeq; WP_011423830.1; NC_007761.1.
DR   AlphaFoldDB; Q2KD13; -.
DR   SMR; Q2KD13; -.
DR   STRING; 347834.RHE_CH00452; -.
DR   EnsemblBacteria; ABC89273; ABC89273; RHE_CH00452.
DR   KEGG; ret:RHE_CH00452; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_2_0_5; -.
DR   OMA; ERRAYCM; -.
DR   SABIO-RK; Q2KD13; -.
DR   Proteomes; UP000001936; Chromosome.
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; Reference proteome.
FT   CHAIN           1..345
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432265"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT   ACT_SITE        255
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT   BINDING         94..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT   BINDING         256..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9JQV3"
SQ   SEQUENCE   345 AA;  36758 MW;  6FA620F0A5C13EA8 CRC64;
     MRWKRTIQLL DVHAEGEIGR VAIGGVPKIP GETIAAQLHW LNTDPKGDEL RRFLCLEPRG
     APIGSVNLLL PARHPDADAA FIILQPDQAH ASSGSNSICV TTALLESGIV EMQEPETIVT
     LETAAGLVKA TATCRDGRCE KVKLTMVPSF VHELDVEIDT PHWGKIKADL CYGGIFYALV
     DVGQINLTIE KANAAGLVQA GMILKELINR DIKVVHPEIP AISGVAYVMF RDTEADGTVR
     TCTTMWPGRA DRSPCGTGNS ANLATLHARG KAKVGDVFTS KSIIGSEFEV GLQAVTEVAG
     RPAVIPTITG RGFTFGLTQV ALDPFDPHPG GFALTDVWGP SAGEI