GRDC_PEPAC
ID GRDC_PEPAC Reviewed; 513 AA.
AC P54935;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Glycine/sarcosine/betaine reductase complex component C subunit beta;
DE Short=Protein PC beta;
DE EC=1.21.4.2;
DE EC=1.21.4.3;
DE EC=1.21.4.4;
GN Name=grdC;
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=al-2 / ATCC 49065 / DSM 3953Z;
RA Luebbers M., Andreesen J.R.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=al-2 / ATCC 49065 / DSM 3953Z;
RX PubMed=8223622; DOI=10.1111/j.1432-1033.1993.tb18307.x;
RA Luebbers M., Andreesen J.R.;
RT "Components of glycine reductase from Eubacterium acidaminophilum. Cloning,
RT sequencing and identification of the genes for thioredoxin reductase,
RT thioredoxin and selenoprotein PA.";
RL Eur. J. Biochem. 217:791-798(1993).
RN [3]
RP PROTEIN SEQUENCE OF 1-23.
RC STRAIN=al-2 / ATCC 49065 / DSM 3953Z;
RX PubMed=1587286; DOI=10.1111/j.1432-1033.1992.tb16903.x;
RA Schraeder T., Andreesen J.R.;
RT "Purification and characterization of protein PC, a component of glycine
RT reductase from Eubacterium acidaminophilum.";
RL Eur. J. Biochem. 206:79-85(1992).
CC -!- FUNCTION: In the first step of glycine, betaine and sarcosine
CC reductases, the substrate is bound to component PB via a Schiff base
CC intermediate. Then the PB-activated substrate is nucleophilically
CC attacked by the selenol anion of component PA to transform it to a
CC carboxymethylated selenoether and the respective amine. By action of
CC component PC, acetyl phosphate is formed, leaving component PA in its
CC oxidized state. Finally component PA becomes reduced by the thioredoxin
CC system to start a new catalytic 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 -!- 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 -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + acetyl phosphate + H2O +
CC trimethylamine = [thioredoxin]-dithiol + glycine betaine + H(+) +
CC phosphate; Xref=Rhea:RHEA:11848, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17750,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:29950, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:58389; EC=1.21.4.4;
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits. Component
CC of the glycine, sarcosine and betaine reductase complexes, together
CC with proteins A and B.
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DR EMBL; L04500; AAB93306.1; -; Genomic_DNA.
DR PIR; S38991; S38991.
DR AlphaFoldDB; P54935; -.
DR SMR; P54935; -.
DR PRIDE; P54935; -.
DR BioCyc; MetaCyc:MON-20604; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0033795; F:betaine reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0030699; F:glycine reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0033794; F:sarcosine reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR045984; DUF5940.
DR InterPro; IPR017236; Gly/sarc/bet/_Rdtase_C_bsu.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF19364; DUF5940; 1.
DR PIRSF; PIRSF037559; Gly_sarc_betain_red_a; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Oxidoreductase.
FT CHAIN 1..513
FT /note="Glycine/sarcosine/betaine reductase complex
FT component C subunit beta"
FT /id="PRO_0000087601"
SQ SEQUENCE 513 AA; 54458 MW; 957DC65C9EB2CC99 CRC64;
MNFPVLKGAG YVLVHTPDMI MHNGTTQTTE KIVNPESEYL KKLPEHLRSF EDVVAYAPNQ
TYIGSMTPEA LGEIAMPWWT EDKKVAGADR YGKLGEIMPQ DEFLALMSAS DVFDLVLFEK
EFIEGAKAKL AAHPVVGNLA ESVNAGVELA EIEKQLSEFH AEGLYNNGKL VGCVKRAHDV
DVNLNSHTML ENLAVKASGV LALANLIAKN NVNPAEVDYI IECSEEACGD MNQRGGGNFA
KALAEMTGCV NATGSDMRGF CAGPTHALIA AAALVKSGVY KNVIIAAGGA TAKLGMNGKD
HVKKEMPILE DCLGGFAVLV SENDGVNPIL RTDLVGRHTV ATGSAPQAVI GSLVLSPLKA
GGLKITDVDK YSVEMQNPDI TKPAGAGDVP EANYKMIAAL AVMGKEIERA DIAAFVEKHG
MVGWAPTQGH IPSGVPYIGF AISDLTEGSV NRTMIVGKGS LFLGRMTNLF DGVSIVAERN
TGKVESGSSV STEEIRKMIA ESMKDFAAHL LAE
