ID   GRDE_PEPAC              Reviewed;         428 AA.
AC   Q9R4G7; O32517;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Glycine reductase complex component B subunits alpha and beta;
DE            EC=1.21.4.2;
DE   AltName: Full=Selenoprotein PB alpha/beta;
DE   Contains:
DE     RecName: Full=Betaine reductase component B subunit beta;
DE   Contains:
DE     RecName: Full=Betaine reductase component B subunit alpha;
GN   Name=grdE;
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 1-33; 85-98;
RP   107-128; 178-190; 243-262 AND 288-297.
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   PROTEIN SEQUENCE OF 1-33, 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   -!- PTM: The peptide chain is cleaved into beta and alpha chains, and the
CC       alpha chain N-terminal cysteine is deaminated and oxidized to form a
CC       reactive pyruvoyl group. {ECO:0000250}.
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DR   EMBL; Y14275; CAA74649.1; -; Genomic_DNA.
DR   PIR; S63507; S63507.
DR   AlphaFoldDB; Q9R4G7; -.
DR   PRIDE; Q9R4G7; -.
DR   KEGG; ag:CAA74649; -.
DR   BioCyc; MetaCyc:MON-20606; -.
DR   BRENDA; 1.21.4.2; 2180.
DR   GO; GO:0030699; F:glycine reductase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR016585; Gly/sarc/bet_Rdtase_B_asu/bsu.
DR   InterPro; IPR015417; Gly_reductase_pB_sua/b.
DR   Pfam; PF09338; Gly_reductase; 1.
DR   PIRSF; PIRSF011588; Gly_sarc_betain_red_a/b; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Pyruvate; Schiff base.
FT   CHAIN           1..241
FT                   /note="Betaine reductase component B subunit beta"
FT                   /id="PRO_0000021372"
FT   CHAIN           242..428
FT                   /note="Betaine reductase component B subunit alpha"
FT                   /id="PRO_0000021373"
FT   ACT_SITE        242
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT   MOD_RES         242
FT                   /note="Pyruvic acid (Cys)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  46263 MW;  6ED9B74B352203D5 CRC64;
     MRLEIGNIFI KDIQFGEQTK VENGVLYVNK DEMIKKLSVI EHIKSVDLDI ARPGESVRIT
     PVKDVIEPRV KVEGPGGIFP GVISKVETDG SGRTHVLKGA AVVTTGKVVG FQEGIVDMSG
     VGAEYTPFSK TLNLVVIAEP EDGIEQHRHE EVLRMVGLNA GVYIGEAGRS VTPDEVKVYE
     TDTIFEGAAK YPNLPKVGYV YMLQTQGLLH DTYVYGVDAK KIVPTILYPT EVMDGAILSG
     NCVSSCDKNP TYVHCNNPMV EELYAMHGKE INFVGVIITN ENVYLADKER SSDWTAKLCK
     FLGLDGAIVS QEGFGNPDTD LIMNCKKIEM EGVKTVISTD EYAGRDGASQ SLADADVRAN
     AVVSNGNANM VIVLPPMDKT IGHIQYIDTI AGGFDGSLRA DGSIEVEIQA ITGATNELGF
     GYLSAKGY