ID   GRDF_PEPAC              Reviewed;         436 AA.
AC   O86186;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   02-JUN-2021, entry version 62.
DE   RecName: Full=Sarcosine reductase complex component B subunit beta;
DE            EC=1.21.4.3;
DE   AltName: Full=Selenoprotein PB beta;
GN   Name=grdF;
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RA   Sonntag D., Soehling B., Andreesen J.R.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In the first step of sarcosine 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 + methylamine
CC         = [thioredoxin]-dithiol + H(+) + phosphate + sarcosine;
CC         Xref=Rhea:RHEA:12825, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22191,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:43474, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57433, ChEBI:CHEBI:59338; EC=1.21.4.3;
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. Component
CC       of the sarcosine reductase complex, together with components A and C.
CC       PB is substrate specific.
CC   -!- SIMILARITY: Belongs to the GrdB/GrdF/GrdH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA76907.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y17872; CAA76907.1; ALT_SEQ; Genomic_DNA.
DR   PIR; T08627; A59190.
DR   GO; GO:0030700; C:glycine reductase complex; IEA:InterPro.
DR   GO; GO:0030699; F:glycine reductase activity; IEA:InterPro.
DR   GO; GO:0033794; F:sarcosine 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="Sarcosine reductase complex component B subunit
FT                   beta"
FT                   /id="PRO_0000087603"
FT   ACT_SITE        350
FT   NON_STD         350
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  46779 MW;  AB18D16D0102F60C CRC64;
     MKKLKVVHYI NNFFAGVGGE EKANIPPEMR EGAVGPGMAL AAALGDEAEV VATVICGDSY
     YGENMDSARK EILEMIKDAQ PDAFVAGPAF NAGRYGVACG SIAKAVEEDL GIPSVTGMYV
     ENPGVDMYRK DIQIIETGNS AADLRNSMPK LAKLVMKKAK GELVGPPEVE GYHMMGIRTN
     FFHEKRGSER AIDMLVNKLN GEKFETEYPM PVFDRVPPNP AVKDMSKVKV AIVTSGGIVP
     HDNPDRIESS SATRYGIYDI TGMDSMSADD FTSIHGGYDR AFVVKDPNLV VPLDVMRDLE
     REGVIGELAN YFVSTTGTGT SVGNAKGFGE SFSKKLIEDG VGAVILTSTU GTCTRCGATM
     VKEIERAGIP VVHLATVVPI SLTIGANRIV PAIGIPHPLG DPALDAKGDK KLRRELVMRG
     LKALQTEVDE QTVFEG