ID   4HYPE_CERS4             Reviewed;         337 AA.
AC   Q3IWG2;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=RSP_3519 {ECO:0000312|EMBL:ABA81122.1};
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
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 involved in a
CC       degradation pathway that converts t4LHyp to alpha-ketoglutarate, which
CC       allows R.sphaeroides to grow on t4LHyp as a sole carbon source.
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   -!- INDUCTION: Is up-regulated when the bacterium is grown on t4LHyp as
CC       sole carbon source. {ECO:0000269|PubMed:24980702}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene loss their ability to
CC       grow on t4LHyp as a sole carbon source. {ECO:0000269|PubMed:24980702}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000144; ABA81122.1; -; Genomic_DNA.
DR   RefSeq; WP_011339379.1; NZ_CP030272.1.
DR   RefSeq; YP_355023.1; NC_007494.2.
DR   AlphaFoldDB; Q3IWG2; -.
DR   SMR; Q3IWG2; -.
DR   STRING; 272943.RSP_3519; -.
DR   EnsemblBacteria; ABA81122; ABA81122; RSP_3519.
DR   GeneID; 67449006; -.
DR   KEGG; rsp:RSP_3519; -.
DR   PATRIC; fig|272943.9.peg.3961; -.
DR   eggNOG; COG3938; Bacteria.
DR   OMA; ERRAYCM; -.
DR   PhylomeDB; Q3IWG2; -.
DR   Proteomes; UP000002703; Chromosome 2.
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..337
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432257"
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         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         257..258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   337 AA;  36831 MW;  7D73A79FE1A28752 CRC64;
     MRVQDVYNVI YTHTEGEPLC IIYSGVPYPA GSTILEKRAF LEENYDWLRK ALMREPRGHA
     DMFGVFLTPP SSRDYDAGLI YIDGKEYSHM CGHGTIAVAM AMVANGLVAR DPSGLTRIRF
     ETTAGLVVAE VAHEGDRVLW TRFENVPAYV AAQDIAFELP GYGPLKADLV WGGNYFGIID
     LRGTSLRIAP ENGSELSRMG LIAREEIRKK VKVQHPTEAH INNLNFVTFW HEPTIEGCLY
     KNVHVFSAGQ LDRSPGGTGT SAMMAYFEAR GVIGLNQPIT SEGLLGSGTF EGCLIGETTL
     GTVRAVRPTV KGTAGMLGTA SWTINREDPV DAGFLVL