ID   4HYPE_SHELP             Reviewed;         333 AA.
AC   A3QFI1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Shew_2363 {ECO:0000312|EMBL:ABO24229.1};
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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). 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=12 mM for trans-4-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 50 sec(-1). {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000606; ABO24229.1; -; Genomic_DNA.
DR   RefSeq; WP_011866160.1; NC_009092.1.
DR   AlphaFoldDB; A3QFI1; -.
DR   SMR; A3QFI1; -.
DR   STRING; 323850.Shew_2363; -.
DR   EnsemblBacteria; ABO24229; ABO24229; Shew_2363.
DR   KEGG; slo:Shew_2363; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_0_0_6; -.
DR   OMA; SHVLWTG; -.
DR   OrthoDB; 559014at2; -.
DR   SABIO-RK; A3QFI1; -.
DR   Proteomes; UP000001558; Chromosome.
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..333
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432275"
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   333 AA;  36112 MW;  06432B8178EBF924 CRC64;
     MLKGTFFCVD AHTCGNPVRL VTSGHPDLKG RTMSEKRQDF LAQYDWIRKA LMFEPRGHDM
     MSGAFLYPPC SDNADAAILF IETSGCLPMC GHGTIGTITA ALESGLLTPK MPGQLTIDVP
     AGQIKVQYQQ TGAKVDWVKI FNVPAYLAHK DVVLDIPGLG PLKIDVSYGG NYYAIVDPQA
     NFPGLRHWSA GDILRWSPIV REVAHRELNC VHPDDPTVNG VSHVLWTGDT ISEGSNGANA
     VFYGDKAIDR SPCGTGTSAR LAQLYSRGEL KVGDEYTHES IIGSQFVGRI EAATKVGAFD
     AIMPSIKGWA RITGHNAITV DDNDPYAFGF QVV