GRDB_SYMTH
ID GRDB_SYMTH Reviewed; 429 AA.
AC Q67KE7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
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=STH2867;
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863;
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD41851.1; -; Genomic_DNA.
DR STRING; 292459.STH2867; -.
DR PRIDE; Q67KE7; -.
DR KEGG; sth:STH2867; -.
DR eggNOG; COG1978; Bacteria.
DR HOGENOM; CLU_053106_0_0_9; -.
DR OMA; NPDHIES; -.
DR Proteomes; UP000000417; 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..429
FT /note="Glycine reductase complex component B subunit gamma"
FT /id="PRO_0000318649"
FT ACT_SITE 344
FT NON_STD 344
FT /note="Selenocysteine"
SQ SEQUENCE 429 AA; 46050 MW; 0F8E58D9D3D6F92B CRC64;
MRIVHYLNQF FGGIGGEEHA GVRPEVRPGP VGPGMALKAA LGDAGEIVAT VICGDSWFNE
NLEEAKATVL ALIRQQNPDL VVAGPAFNAG RYGMACGAVA EVVSKELGIP VVTGMFLENP
GVEVYRRYAW VVETGNSAAS MRTAIPAMAA LIRRLAAGQE PEPGTYLERG LRVNTFAAER
GSARAVEMLV RKLKGEPYTT EYPMPSFDRV PPNPPVKDLS KAKIALVTSG GIVPKGNPDH
IESSSASKYG KYYLGDLDDL TAETHQTAHG GYDPTYANAD ADRVLPVDVM RELEREGVIG
KLHDYWYATV GNGTSVANAR AYAREIAEDL KKYEVDAVIL TSTUGTCTRC GATMVKEIER
AGIPVVHVCT VVPISLTVGA NRIVPAVAIP HPLGNPALPP DEERTLRRRL VMKALQALTT
PVDGQTVFE
