ID   GRDB_PEPAC              Reviewed;         438 AA.
AC   Q9R4G8; O32519; O53034;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 67.
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 acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30; 200-215;
RP   229-238; 241-251 AND 327-334.
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=10091582; DOI=10.1046/j.1432-1327.1999.00107.x;
RA   Wagner M., Sonntag D., Grimm R., Pich A., Eckerskorn C., Soehling B.,
RA   Andreesen J.R.;
RT   "Substrate-specific selenoprotein B of glycine reductase from Eubacterium
RT   acidaminophilum. Biochemical and molecular analysis.";
RL   Eur. J. Biochem. 260:38-49(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-438.
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RA   Luebbers M.;
RT   "Eubacterium acidaminophilum selenoprotein B.";
RL   Thesis (1993), University of Goettingen, Germany.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-30, AND CHARACTERIZATION.
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=8529639; DOI=10.1111/j.1432-1033.1995.184_c.x;
RA   Meyer M., Granderath K., Andreesen J.R.;
RT   "Purification and characterization of protein PB of betaine reductase and
RT   its relationship to the corresponding proteins glycine reductase and
RT   sarcosine reductase from Eubacterium acidaminophilum.";
RL   Eur. J. Biochem. 234:184-191(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; Y14275; CAA74651.1; -; Genomic_DNA.
DR   EMBL; L04500; AAB93302.2; -; Genomic_DNA.
DR   PIR; S63509; S63509.
DR   PRIDE; Q9R4G8; -.
DR   KEGG; ag:CAA74651; -.
DR   BioCyc; MetaCyc:MON-20601; -.
DR   GO; GO:0030700; C:glycine reductase complex; IEA:InterPro.
DR   GO; GO:0030699; F:glycine reductase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR023193; EPSP_synthase_CS.
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.
DR   PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Selenocysteine.
FT   CHAIN           1..438
FT                   /note="Glycine reductase complex component B subunit gamma"
FT                   /id="PRO_0000087600"
FT   ACT_SITE        350
FT   NON_STD         350
FT                   /note="Selenocysteine"
SQ   SEQUENCE   438 AA;  47369 MW;  429C1C1AD7001908 CRC64;
     MSKIRVVHYI NQFFAGVGGE EKADIEPFIA ESLPPVSQSL SNLIKDEAEV VGTVVCGDSY
     FGENLVEAKN RILEMIKSFN PDIVVAGPAF NAGRYGVAAA TVTKAVQDEL GIPAVTGMYI
     ENPGADMFKK YAYIISTGNS AAAMRTALPA MAKFAMKLAK GEEIGGPVAE GYIERGIRFN
     MFKEDRGAKR AVAMLVKKLK GEEYETEYPM PSFDKVEPGK AIKDMSKAKI AIVTSGGIVP
     KGNPDRIESS SASKYGKYDI QGIDDLTSEG WETAHGGHDP IYANEDADRV IPVDVLRDME
     KEGVIGELHR YFYSTTGNGT AVASSKKFAE EFTKELVADG VDAVILTSTU GTCTRCGASM
     VKEIERSGIP VVHIATVTPI SLTVGANRIV PAIAIPHPLG NPALSHEEEK ALRRKIVEKA
     LEALQTEVEE QTVFERNY