PRAC_ACESD
ID PRAC_ACESD Reviewed; 335 AA.
AC E3PTZ4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Proline racemase {ECO:0000303|PubMed:20937090, ECO:0000303|PubMed:24314397};
DE Short=PR {ECO:0000303|PubMed:24314397};
DE EC=5.1.1.4 {ECO:0000269|PubMed:24314397, ECO:0000269|PubMed:5722267};
DE AltName: Full=AsProR {ECO:0000305};
DE AltName: Full=CsPR {ECO:0000303|PubMed:24314397};
GN Name=prdF {ECO:0000303|PubMed:20937090, ECO:0000312|EMBL:CBH22348.1};
GN OrderedLocusNames=CLOST_2228 {ECO:0000312|EMBL:CBH22348.1};
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=5722267; DOI=10.1021/bi00851a026;
RA Cardinale G.J., Abeles R.H.;
RT "Purification and mechanism of action of proline racemase.";
RL Biochemistry 7:3970-3978(1968).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INHIBITION
RP STUDY.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=24314397; DOI=10.1016/j.bmcl.2013.10.061;
RA Harty M., Nagar M., Atkinson L., Legay C.M., Derksen D.J., Bearne S.L.;
RT "Inhibition of serine and proline racemases by substrate-product
RT analogues.";
RL Bioorg. Med. Chem. Lett. 24:390-393(2014).
CC -!- FUNCTION: Catalyzes the reversible interconversion of L- and D-proline
CC (PubMed:5722267, PubMed:24314397). Likely functions as the proline
CC racemase necessary for D-proline generation in order to discriminate it
CC from the L-proline used for protein synthesis (PubMed:20937090).
CC {ECO:0000269|PubMed:24314397, ECO:0000269|PubMed:5722267,
CC ECO:0000303|PubMed:20937090}.
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:24314397, ECO:0000269|PubMed:5722267};
CC -!- ACTIVITY REGULATION: Inhibited by pyrrole-2-carboxylate in vitro.
CC {ECO:0000269|PubMed:5722267}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for L-proline {ECO:0000269|PubMed:5722267};
CC KM=3.8 mM for D-proline {ECO:0000269|PubMed:5722267};
CC KM=7.2 mM for L-proline {ECO:0000269|PubMed:24314397};
CC Note=kcat is 64 sec(-1) with L-proline as substrate.
CC {ECO:0000269|PubMed:24314397};
CC -!- MISCELLANEOUS: Differs from other amino acid racemases in that no
CC requirement for pyridoxal phosphate could be shown.
CC {ECO:0000269|PubMed:5722267}.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; FP565809; CBH22348.1; -; Genomic_DNA.
DR SMR; E3PTZ4; -.
DR STRING; 1511.CLOST_2228; -.
DR EnsemblBacteria; CBH22348; CBH22348; CLOST_2228.
DR KEGG; cst:CLOST_2228; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_0_0_9; -.
DR OMA; SHVLWTG; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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..335
FT /note="Proline racemase"
FT /id="PRO_0000454288"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 335 AA; 36827 MW; F4F280DDE23AAFB6 CRC64;
MKFSKGIHAI DSHTMGEPTR IVVGGIPQIN GETMADKKKY LEDNLDYVRT ALMHEPRGHN
DMFGSIITSS NNKEADFGII FMDGGGYLNM CGHGSIGAAT VAVETGMVEM VEPVTNINME
APAGLIKAKV MVENEKVKEV SITNVPSFLY MEDAKLEVPS LNKTITFDIS FGGSFFAIIH
AKELGVKVET SQVDVLKKLG IEIRDLINEK IKVQHPELEH IKTVDLVEIY DEPSNPEATY
KNVVIFGQGQ VDRSPCGTGT SAKLATLYKK GHLKIDEKFV YESITGTMFK GRVLEETKVG
EFDAIIPEIT GGAYITGFNH FVIDPEDPLK YGFTV
