ID   GCSPA_CARHZ             Reviewed;         444 AA.
AC   Q3AET5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=CHY_0491;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB15168.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AET5; -.
DR   SMR; Q3AET5; -.
DR   STRING; 246194.CHY_0491; -.
DR   KEGG; chy:CHY_0491; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_9; -.
DR   InParanoid; Q3AET5; -.
DR   OrthoDB; 9771867at2; -.
DR   Proteomes; UP000002706; 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..444
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000045640"
SQ   SEQUENCE   444 AA;  48908 MW;  A9A0197BAEEB89D9 CRC64;
     MKYTPHTPDE VREMLSSLGL SSIEELFSDI PEEVKLKRPL NLPSGMSELE VKKHLANLAA
     KNGSADKYTV FLGAGVYDHY VPAVVNHILL RSEFYTAYTP YQAEMSQGVL QSIFEYQTMI
     CELTGLDITN ASMYDGGSAL AEAALMAVSQ TRRDKVLVLA TVHPEYRSVV KTYTWGPEIE
     VVEVPYKSGT VDLEKLEELI DDKTAAVLVQ HPNFFGQLEP VEEISRLIHA QKGLLVVAVD
     PISLGILKPP AEYGADIAVG DGQALGNGLA FGGPHLGFFA ARKDLARRMP GRLVGLTTDK
     EGNRGFVLTL QAREQHIRRE KATSNICSNQ ALNALAATVY LATVGKKGLK EIALQSLQKA
     HYAFERLIGE GYEPLFSGPF FKEFVVKVKN EEEITQKLLK HHILAGPGIS RFYPELAPAL
     MIAVTEKRTR EEIDNLVEVL GGDR
//