ID   Y2339_CHRSD             Reviewed;         361 AA.
AC   Q1QV19;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Protein Csal_2339;
DE            EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN   OrderedLocusNames=Csal_2339 {ECO:0000312|EMBL:ABE59689.1};
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
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: In vitro, catalyzes the epimerization of trans-4-hydroxy-L-
CC       proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), albeit with very
CC       low efficiency. The physiological substrate may be different. Displays
CC       neither proline racemase activity nor t3LHyp dehydratase activity.
CC       {ECO:0000269|PubMed:24980702, ECO:0000305}.
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=2.5 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 0.070 sec(-1) for t4LHyp epimerization.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000285; ABE59689.1; -; Genomic_DNA.
DR   RefSeq; WP_011507635.1; NC_007963.1.
DR   AlphaFoldDB; Q1QV19; -.
DR   SMR; Q1QV19; -.
DR   STRING; 290398.Csal_2339; -.
DR   EnsemblBacteria; ABE59689; ABE59689; Csal_2339.
DR   KEGG; csa:Csal_2339; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_2_0_6; -.
DR   OMA; IMESEEY; -.
DR   OrthoDB; 559014at2; -.
DR   SABIO-RK; Q1QV19; -.
DR   Proteomes; UP000000239; 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..361
FT                   /note="Protein Csal_2339"
FT                   /id="PRO_0000432254"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT   BINDING         92..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT   BINDING         259..260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B9K4G4"
SQ   SEQUENCE   361 AA;  38982 MW;  AFE9E9FF0049304E CRC64;
     MSEELTLQLI DLHAGGDVSR IVTGGIDPLP GNTVREKMEY LREDADGLRQ LLLSEPYGIP
     EMSVDLLVPA SDPEAEVGYI IMEVMGYPIY SGSNTICTAT AVLESGLVPK REGHQRFILE
     SAAGLVHIEA RVENGVVEAI TCEGLPSYID TYRASIHVPS VGDVTYSVAY SGGFYAMVDA
     AELGFSLNRD EEARLAECAH AIVEAIQAER GFSHYTLGDV GPLPFLHFMG PVEQVADGFF
     RSRSTTYVHP GVICRSTTGT GTSARLALMH HEGTLQPGDK LETVSLRGTG FIGEFTGSRQ
     EGDHRVAENT ITGKAHMLAR SDIVINCNDP LVECGSLHHI LTSGHRRTEA LPVEEEVSLS
     D