ID   PRDB_ACESD              Reviewed;         242 AA.
AC   Q9Z4Q7; E3PTZ7;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=D-proline reductase subunit gamma;
DE            EC=1.21.4.1 {ECO:0000269|PubMed:10085076};
DE   AltName: Full=D-proline reductase 26 kDa subunit;
GN   Name=prdB; OrderedLocusNames=CLOST_2232;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19; 51-80; 87-102;
RP   140-161 AND 231-242, SELENOCYSTEINE AT SEC-152, SUBUNIT, SUBCELLULAR
RP   LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX   PubMed=10085076; DOI=10.1074/jbc.274.13.8445;
RA   Kabisch U.C., Graentzdoerffer A., Schierhorn A., Ruecknagel K.P.,
RA   Andreesen J.R., Pich A.;
RT   "Identification of D-proline reductase from Clostridium sticklandii as a
RT   selenoenzyme and indications for a catalytically active pyruvoyl group
RT   derived from a cysteine residue by cleavage of a proprotein.";
RL   J. Biol. Chem. 274:8445-8454(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
CC   -!- FUNCTION: D-proline reductase catalyzes the reductive cleavage of a C-N
CC       bond in D-proline resulting in the formation of 5-aminovalerate. The
CC       alpha subunit has been shown to bind D-proline, presumably via the
CC       pyruvoyl group. {ECO:0000269|PubMed:10085076}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminopentanoate + [PrdC protein]-Se-L-selenocysteinyl-S-L-
CC         cysteine = [PrdC protein]-L-selenocysteine/L-cysteine + D-proline;
CC         Xref=Rhea:RHEA:12737, Rhea:RHEA-COMP:14983, Rhea:RHEA-COMP:14984,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30000, ChEBI:CHEBI:57726,
CC         ChEBI:CHEBI:142235, ChEBI:CHEBI:356010; EC=1.21.4.1;
CC         Evidence={ECO:0000269|PubMed:10085076};
CC   -!- SUBUNIT: Consists of 3 subunits of 23, 26 and 45 kDa (alpha, gamma and
CC       beta respectively). The molecular weight of the complex is
CC       approximately 870 kDa, suggesting a decameric structure, if all 3
CC       subunits are present in equal stoichiometry.
CC       {ECO:0000269|PubMed:10085076}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10085076}.
CC   -!- PTM: This subunit is carbonylated in vitro on an unidentified residue.
CC   -!- MISCELLANEOUS: The reaction mechanism first involves the formation of
CC       an adduct (and not a Schiff base) between the nitrogen of proline and
CC       the pyruvoyl group of the alpha subunit. The selenol anion of
CC       selenocysteine in PrdB nucleophilically attacks the alpha-carbon,
CC       resulting in cleavage of the N-C bond of the proline ring. This
CC       intermediate is then transformed to the oxidized gamma subunit
CC       containing a mixed selenide/sulfide group and to the 5-aminovalerate
CC       adduct of the alpha subunit. The final product, 5-aminovalerate, is
CC       formed by hydrolysis. Subsequently, the selenide-sulfide group of PrdB
CC       is reduced, but the natural electron donating system for D-proline
CC       reductase is unknown.
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DR   EMBL; AJ130879; CAB38127.2; -; Genomic_DNA.
DR   EMBL; FP565809; CBH22351.1; -; Genomic_DNA.
DR   STRING; 1511.CLOST_2232; -.
DR   PRIDE; Q9Z4Q7; -.
DR   KEGG; cst:CLOST_2232; -.
DR   eggNOG; COG1978; Bacteria.
DR   HOGENOM; CLU_085018_0_0_9; -.
DR   OMA; FFGAPTN; -.
DR   BioCyc; MetaCyc:PRDBST-MON; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050002; F:D-proline reductase (dithiol) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR022787; D_pro_red_PrdB.
DR   InterPro; IPR010187; Various_sel_PB.
DR   Pfam; PF07355; GRDB; 1.
DR   TIGRFAMs; TIGR04483; D_pro_red_PrdB; 1.
DR   TIGRFAMs; TIGR01918; various_sel_PB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Oxidoreductase; Reference proteome;
KW   Selenocysteine.
FT   CHAIN           1..242
FT                   /note="D-proline reductase subunit gamma"
FT                   /id="PRO_0000240012"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   NON_STD         152
FT                   /note="Selenocysteine"
SQ   SEQUENCE   242 AA;  25812 MW;  529A941DA88229C5 CRC64;
     MSDLTVVKGL QSEIYVPITP PPVWTPVTKE LKDMTVALVT AAGVHMKADK RFNLAGDFSF
     RVIPGDASVN DMMVSHGGYD NGDVNKDINC MFPIDPMRTL AKEGFIKALA PINIGFMGGG
     GDQKKFSEET GPEIARQLKE EGVDAVLLTA GUGTCHRSAV IVQRAIEESG IPTIIIAALP
     PVVRQNGTPR AVAPLVPMGA NAGEPNNPEM QKAICTDSLK QLVEIPSAGK IVPLPYEYVA
     KV