ID   4HYPE_PSYCK             Reviewed;         332 AA.
AC   Q1QBF3;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Pcryo_1219 {ECO:0000312|EMBL:ABE75000.1};
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) 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       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   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000323; ABE75000.1; -; Genomic_DNA.
DR   RefSeq; WP_011513552.1; NC_007969.1.
DR   AlphaFoldDB; Q1QBF3; -.
DR   SMR; Q1QBF3; -.
DR   STRING; 335284.Pcryo_1219; -.
DR   KEGG; pcr:Pcryo_1219; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_1_0_6; -.
DR   OMA; SHVLWTG; -.
DR   Proteomes; UP000002425; 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.
FT   CHAIN           1..332
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432285"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         93..94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         243..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   332 AA;  35949 MW;  7F7AEDC8E2CC49E2 CRC64;
     MASSLFNFKI IDSHTGGEPT RMVYDGFPDL VGDTIQDKLQ SFKQNFDHLR QSIILEPRGN
     DVLVGALLLP ASHPKATAGV IFFNNAGYLG MCGHGTIGVI VSLAYQQKIS AGVHWLETPV
     GLVKATLHDD GSCSVQNVPS YRYKKQVEVH VPELGLIRGD IAWGGNWFFL VSEHGQDIQA
     SNVKQLTQVT MQIKQALVAA NITGENSSEI DHIELFADSD DTQVDSKNFV LCPGSAYDRS
     PCGTGTSAKL ACLAADNKLA PEQLWQQQGV VGSVFTGSYQ YASELNTTLK NPAGAAYPEQ
     TIIPTICGHA YVCAETTLIM QEDDPFKWGI PS