ID   PRAC_CLOD6              Reviewed;         335 AA.
AC   Q17ZY4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Proline racemase;
DE            EC=5.1.1.4;
GN   OrderedLocusNames=CD630_32370;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of L- and D-proline.
CC       Plays an important role in the regulation of intra- and extracellular
CC       amino acid pools, allowing the bacterium to profit from host precursors
CC       and enzymatic pathways. Strong B-cell mitogen.
CC       {ECO:0000250|UniProtKB:A8DEZ8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline = D-proline; Xref=Rhea:RHEA:10680,
CC         ChEBI:CHEBI:57726, ChEBI:CHEBI:60039; EC=5.1.1.4;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; AM180355; CAJ70135.1; -; Genomic_DNA.
DR   RefSeq; WP_003422090.1; NZ_CP010905.2.
DR   RefSeq; YP_001089754.1; NC_009089.1.
DR   AlphaFoldDB; Q17ZY4; -.
DR   SMR; Q17ZY4; -.
DR   STRING; 272563.CD630_32370; -.
DR   EnsemblBacteria; CAJ70135; CAJ70135; CD630_32370.
DR   GeneID; 66355657; -.
DR   KEGG; cdf:CD630_32370; -.
DR   KEGG; pdc:CDIF630_03533; -.
DR   PATRIC; fig|272563.120.peg.3419; -.
DR   eggNOG; COG3938; Bacteria.
DR   OMA; SHVLWTG; -.
DR   PhylomeDB; Q17ZY4; -.
DR   BioCyc; PDIF272563:G12WB-3404-MON; -.
DR   BRENDA; 5.1.1.4; 1473.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0018112; F:proline racemase 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   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..335
FT                   /note="Proline racemase"
FT                   /id="PRO_0000354023"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        255
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   335 AA;  36221 MW;  C1C7BD9E6E3FAB86 CRC64;
     MKFSRSIQAI DSHTAGEATR IVVGGIPNIK GNSMPEKKEY LEENLDYLRT AIMLEPRGHN
     DMFGSVMTQP CCPDADFGII FMDGGGYLNM CGHGTIGAMT AAIETGVVPA VEPVTHVVME
     APAGIIRGDV TVVDGKAKEV SFLNVPAFLY KEGVEVDLPG VGTVKFDISF GGSFFAIIHA
     SQLGLKIEPQ NAGKLTELAM KLRDIINEKI EIQHPTLAHI KTVDLVEIYD EPTHPEATYK
     NVVIFGQGQV DRSPCGTGTS AKLATLHAKG ELKVGEKFVY ESILGTLFKG EIVEETKVAD
     FNAVVPKITG SAYITGFNHF VIDEEDPLKH GFILK