GRDE_ACESD
ID GRDE_ACESD Reviewed; 430 AA.
AC Q9EV94; E3PXR7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 74.
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; OrderedLocusNames=CLOST_1110;
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=11271425; DOI=10.1007/s002030000232;
RA Graentzdoerffer A., Pich A., Andreesen J.R.;
RT "Molecular analysis of the grd-operon encoded proteins of the glycine
RT reductase and thioredoxin system from Clostridium sticklandii.";
RL Arch. Microbiol. 175:8-18(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
RN [3]
RP PROTEIN SEQUENCE OF 1-10 AND 243-253, PROTEOLYTIC PROCESSING IN VITRO, AND
RP MUTAGENESIS OF CYS-242.
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=11422384; DOI=10.1046/j.1432-1327.2001.02257.x;
RA Bednarski B., Andreesen J.R., Pich A.;
RT "In vitro processing of the proproteins grdE of protein B of glycine
RT reductase and prdA of D-proline reductase from Clostridium sticklandii:
RT formation of a pyruvoyl group from a cysteine residue.";
RL Eur. J. Biochem. 268:3538-3544(2001).
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 -!- 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}.
CC -!- MISCELLANEOUS: The protein sequence in PubMed:11422384 comes from
CC protein overexpressed and processed in E.coli.
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DR EMBL; AJ276209; CAC14299.1; -; Genomic_DNA.
DR EMBL; FP565809; CBH21232.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EV94; -.
DR STRING; 1511.CLOST_1110; -.
DR PRIDE; Q9EV94; -.
DR EnsemblBacteria; CBH21232; CBH21232; CLOST_1110.
DR KEGG; cst:CLOST_1110; -.
DR eggNOG; ENOG502Z7RC; Bacteria.
DR HOGENOM; CLU_050376_0_0_9; -.
DR OMA; EYTPFSK; -.
DR Proteomes; UP000007041; Chromosome.
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; Reference proteome.
FT CHAIN 1..241
FT /note="Betaine reductase component B subunit beta"
FT /id="PRO_0000240008"
FT CHAIN 242..430
FT /note="Betaine reductase component B subunit alpha"
FT /id="PRO_0000240009"
FT ACT_SITE 242
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000305"
FT MOD_RES 242
FT /note="Pyruvic acid (Cys)"
FT /evidence="ECO:0000305"
FT MUTAGEN 242
FT /note="C->A: No in vitro processing occurs."
FT /evidence="ECO:0000269|PubMed:11422384"
FT MUTAGEN 242
FT /note="C->S,T: In vitro processing occurs more slowly than
FT in wild-type."
FT /evidence="ECO:0000269|PubMed:11422384"
FT CONFLICT 251
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 46476 MW; 9172078AC843A8EA CRC64;
MRLEVGNIFI KDIQFGDSTK VENGVLYVNK QELISELSSD EHIKSIDMEI VRPGESVRIA
PVKDVIEPRV KVEGNGGIFP GFLSKVDTVG EGKTNVLKGA AVVTTGKVVG FQEGIIDMTG
PGADYTPFSK TCNVVIIAEP VDGLKQHDHE AALRMVGLKA GKYLGEAGRN ITPDEVKVYE
TKPIFESVKE YPNLPKVAYV YMLQTQGLLH DTYVYGVDAK KIIPTLIYPT EVMDGAILSG
NCVSACDKNP TYVHMNNPVI HDLYELHGKE YNFVGVIITN ENVYLADKER SSNWTAKMAE
YLGLDGVIIS EEGFGNPDTD LIMNCKKITK KGIKTVILTD EYAGRDGASQ SLADADAAAD
ACVTGGNANM TIVLPKLDKI IGHVSKDVID VIAGGFDGSL RADGSIEVEI QAITGATSEV
GFNKMTAKTY
