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Database: UniProt
Entry: A0A0J1DLU0_9FIRM
LinkDB: A0A0J1DLU0_9FIRM
Original site: A0A0J1DLU0_9FIRM 
ID   A0A0J1DLU0_9FIRM        Unreviewed;       446 AA.
AC   A0A0J1DLU0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN   ORFNames=AA931_08365 {ECO:0000313|EMBL:KLU39947.1};
OS   Peptococcaceae bacterium 1109.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1655638 {ECO:0000313|EMBL:KLU39947.1, ECO:0000313|Proteomes:UP000036486};
RN   [1] {ECO:0000313|EMBL:KLU39947.1, ECO:0000313|Proteomes:UP000036486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1109 {ECO:0000313|EMBL:KLU39947.1};
RA   Town J.R., Dumonceaux T.J.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC       Rule:MF_00712}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC         Rule:MF_00712};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00712}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLU39947.1}.
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DR   EMBL; LDJB01000002; KLU39947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J1DLU0; -.
DR   STRING; 1655638.AA931_08365; -.
DR   PATRIC; fig|1655638.3.peg.1677; -.
DR   Proteomes; UP000036486; Unassembled WGS sequence.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42806; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR   PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00712}.
FT   DOMAIN          1..441
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   446 AA;  48573 MW;  9CC9BCCF2F4DAB1C CRC64;
     MRYIPMTDQD REAMLASMGL SSTEELFADI PEHLRTAGGL DLPPALSEAE LIRHMKALAS
     KNTNLEDTIS FMGGGAYDHL IPAIVKHLIS RGEFLTAYTP YQAEISQGVL QSIFEYQTLI
     AELTGMEAAN ASMYDGATAL AEAALMACNA TRRNVVVLPD NLHPEWQEVC ELYLKNQDVE
     IKYLPYLEGA GTIDHEALQS LDEKSIACVV VQQPNFFGLV EDVDPISEFV HSAGGLLVMA
     VDPISLGLLK SPGEYGADIV VGDGQSLGNT MSFGGPSLGF FATTGKLVRR MPGRIVGETV
     DADGRRGFVL TLQTREQHIR REKATSNICS NQALNALAAA IYLSVLGKEG FKEVAYHCLQ
     KTAYLRRRLS EATPFKEKFT APAFREFVVT GPVDWEAVNE ALLKDGFLGG LPLKRFGMAD
     AALFAVTEAR TKDEIDRLVE LLGGMS
//
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