ID   GCSPA_COPPD             Reviewed;         435 AA.
AC   B5Y9D4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712};
GN   OrderedLocusNames=COPRO5265_1070;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS   BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC   Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus strain
RT   ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-2008) 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:0000255|HAMAP-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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00712}.
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DR   EMBL; CP001145; ACI17103.1; -; Genomic_DNA.
DR   RefSeq; WP_012543755.1; NC_011295.1.
DR   AlphaFoldDB; B5Y9D4; -.
DR   SMR; B5Y9D4; -.
DR   STRING; 309798.COPRO5265_1070; -.
DR   KEGG; cpo:COPRO5265_1070; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_9; -.
DR   OrthoDB; 9771867at2; -.
DR   Proteomes; UP000001732; Chromosome.
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; Reference proteome.
FT   CHAIN           1..435
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000147981"
SQ   SEQUENCE   435 AA;  48463 MW;  663DD22E41615B15 CRC64;
     MRYVPHTKEE IKAMLEAVGL RNVDELFSDI PTEALLKRHL QVEGGWDEEQ LRAYFRKAAS
     SIPDANSAVY FLGGGVYDHY VPSAVDKIIA LPEFYTAYTP YQAEISQGTL QAMFEYQSLI
     CELTGMEVAN GSLYDGASAV AEAVLMAMRI NGKRRVLVSE CVHPDIIEVL RTYQLGQDFE
     ILTLPQKEGV TDLSELEDLS NVSCLVMQNP NYYGFLENMN QASELIHKAG GLFVAAVDPL
     SLGVLKSPHE YGADVVVGEG QSLGNHMSYG GPHFGFFATK MDYIRYMPGR MAGQTVDVDG
     RVGYVLTLQT REQHIRREKA TSNITSNHWL MALASAVYLS LMGGSLPELG QTILNRSTYL
     AQKLASVGYP LWQRQYFFKE FPIKARDAEA VQEALADSGY YVGPVIDEHT LLVAVTEKRT
     KEHMDKLIEL MEGLR
//