ID   GRDB_PEPLI              Reviewed;         436 AA.
AC   P52217;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Glycine reductase complex component B subunit gamma;
DE            EC=1.21.4.2;
DE   AltName: Full=Selenoprotein PB gamma;
GN   Name=grdB;
OS   Peptoclostridium litorale (Clostridium litorale).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49638 / DSM 5388 / W6;
RX   PubMed=8529640; DOI=10.1111/j.1432-1033.1995.192_c.x;
RA   Kreimer S., Andreesen J.R.;
RT   "Glycine reductase of Clostridium litorale. Cloning, sequencing, and
RT   molecular analysis of the grdAB operon that contains two in-frame TGA
RT   codons for selenium incorporation.";
RL   Eur. J. Biochem. 234:192-199(1995).
CC   -!- FUNCTION: In the first step of glycine reductase, the substrate is
CC       bound to component PB via a Schiff base intermediate. Then the PB-
CC       activated substrate is nucleophilically attacked by the selenol anion
CC       of component PA to transform it to a carboxymethylated selenoether and
CC       the respective amine. By action of component PC, acetyl phosphate is
CC       formed, leaving component PA in its oxidized state. Finally component
CC       PA becomes reduced by the thioredoxin system to start a new catalytic
CC       cycle of reductive deamination.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + acetyl phosphate + H2O + NH4(+) =
CC         [thioredoxin]-dithiol + glycine + H(+) + phosphate;
CC         Xref=Rhea:RHEA:12232, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22191,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29950, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57305; EC=1.21.4.2;
CC   -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC       Component of the glycine reductase complex, together with components A
CC       and C. PB is substrate specific.
CC   -!- SIMILARITY: Belongs to the GrdB/GrdF/GrdH family. {ECO:0000305}.
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DR   EMBL; U24268; AAC43574.2; -; Genomic_DNA.
DR   PIR; S63988; S63988.
DR   PRIDE; P52217; -.
DR   GO; GO:0030700; C:glycine reductase complex; IEA:InterPro.
DR   GO; GO:0030699; F:glycine reductase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR010186; Gly_red_sel_B.
DR   InterPro; IPR010187; Various_sel_PB.
DR   Pfam; PF07355; GRDB; 1.
DR   TIGRFAMs; TIGR01917; gly_red_sel_B; 1.
DR   TIGRFAMs; TIGR01918; various_sel_PB; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Selenocysteine.
FT   CHAIN           1..436
FT                   /note="Glycine reductase complex component B subunit gamma"
FT                   /id="PRO_0000087598"
FT   ACT_SITE        350
FT   NON_STD         350
FT                   /note="Selenocysteine"
SQ   SEQUENCE   436 AA;  46600 MW;  997AEDCCCD1F0E89 CRC64;
     MGKLRVVHYI NQFFAGIGGE EKADIAPFVA EELPPISQNL DKLLGEDAEV VATVVCGDSF
     FGENLETAQA TVLEMVKGAS PDLFIAGPAF NAGRYGVAAG AITKAVQDTL GIPAVTGMYI
     ENPGADMYKK SVYVMSTADS AAGMRKSLPA LAKFALKYAK GEEIGSPAEE GYIERGIRVN
     GFKEDRGAKR AVAMLVKKLK GEEFVTEYPM PVFDNVVPGR AIVNMSKAKI AIVTSGGIVP
     KGNPDRIESS SASKYGKYDI DGVDDLTSEG WETAHGGHDP VYANEDADRV IPVDVLRDME
     KEGVIGELHR YFYSTTGNGT AVLSSKQFAK EFTQELMAAG VDAVILTSTU GTCTRCGATM
     VKEIERSGIP VVHICTVTPI ALTVGANRIV PAIAIPHPLG DPALSPAEEK ALRRKIVEKS
     LKALETEIEE QTVFED