ID   GRDB_CARHZ              Reviewed;         435 AA.
AC   Q3A9J4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 72.
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; OrderedLocusNames=CHY_2393;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GrdB/GrdF/GrdH family. {ECO:0000305}.
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DR   EMBL; CP000141; ABB15736.1; -; Genomic_DNA.
DR   STRING; 246194.CHY_2393; -.
DR   PRIDE; Q3A9J4; -.
DR   KEGG; chy:CHY_2393; -.
DR   eggNOG; COG1978; Bacteria.
DR   HOGENOM; CLU_053106_0_0_9; -.
DR   OMA; NPDHIES; -.
DR   Proteomes; UP000002706; Chromosome.
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; Reference proteome; Selenocysteine.
FT   CHAIN           1..435
FT                   /note="Glycine reductase complex component B subunit gamma"
FT                   /id="PRO_0000318647"
FT   ACT_SITE        350
FT   NON_STD         350
FT                   /note="Selenocysteine"
SQ   SEQUENCE   435 AA;  46175 MW;  024A82C9B37195F7 CRC64;
     MAKFRVVHYL NQFFGQIGGE EKADTAPLKK DGPVGPGTAL NGAFKGEAEV VGTVICGDSY
     FAENMEEALK QILSMIKEYN PDLVVAGPAF NAGRYGTACG AVAEAVVKNL GIPAVTGMYP
     ENPGVEMYKK SVYIIATADS AIGMRNAIPK MAALGLKLLK KEEIGTPEQE GYIARGIRKN
     YFAEERGAKR AVDMLIAKIK GENFTTELPM PAFDRVPPNP AIKDLSKATI ALVTSGGIVP
     KGNPDRIESS SASKFGKYSI AGVKDLTSDT FETAHGGYDP VYANQDADRV LPVDVLREME
     AEGKIGKLHD YYYATVGNGT SVANAAKFGQ AIAADLKASG VDAVILTSTU GTCTRCGAAM
     VKEIERAGIP VVHMCTIVPI SKTVGANRIV PTVAIPHPLG NPALPADEEK ALRRKLVEKA
     LKALTTEVEG QTVFD