ID   PRAC_CLODI              Reviewed;         335 AA.
AC   A8DEZ8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Proline racemase;
DE            EC=5.1.1.4;
DE   AltName: Full=CdPRAC;
OS   Clostridioides difficile (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=1496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND ROLE IN VIRULENCE.
RC   STRAIN=ATCC 4325 / VPI 10463;
RX   PubMed=17849014; DOI=10.1371/journal.pone.0000885;
RA   Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A.,
RA   Minoprio P.;
RT   "Molecular and structural discrimination of proline racemase and
RT   hydroxyproline-2-epimerase from nosocomial and bacterial pathogens.";
RL   PLoS ONE 2:E885-E885(2007).
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:0000269|PubMed:17849014}.
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         Evidence={ECO:0000269|PubMed:17849014};
CC   -!- ACTIVITY REGULATION: Inhibited by pyrrole-2-carboxylic acid (PYC).
CC       {ECO:0000269|PubMed:17849014}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=60.2 mM for L-proline {ECO:0000269|PubMed:17849014};
CC         KM=46.7 mM for D-proline {ECO:0000269|PubMed:17849014};
CC         Vmax=1.35 uM/sec/mg enzyme with L-proline as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:17849014};
CC         Vmax=0.85 uM/sec/mg enzyme with D-proline as substrate (at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:17849014};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This enzyme does not require pyridoxal phosphate (PLP)
CC       as a cofactor.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; EF495346; ABS82398.1; -; Genomic_DNA.
DR   RefSeq; WP_003422090.1; NZ_WUUI01000016.1.
DR   AlphaFoldDB; A8DEZ8; -.
DR   SMR; A8DEZ8; -.
DR   GeneID; 66355657; -.
DR   OMA; SHVLWTG; -.
DR   BRENDA; 5.1.1.4; 1473.
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   1: Evidence at protein level;
KW   Isomerase.
FT   CHAIN           1..335
FT                   /note="Proline racemase"
FT                   /id="PRO_0000354024"
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