ID   GCSPA_CHLPM             Reviewed;         443 AA.
AC   A4SG06;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=Cvib_1404;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-2007) 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; CP000607; ABP37415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4SG06; -.
DR   SMR; A4SG06; -.
DR   STRING; 290318.Cvib_1404; -.
DR   KEGG; pvi:Cvib_1404; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_10; -.
DR   OrthoDB; 9801272at2; -.
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.
FT   CHAIN           1..443
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000083223"
SQ   SEQUENCE   443 AA;  47720 MW;  7DF81451CE9646F5 CRC64;
     MPFIINTDSD RAEMLAAAGA ASFNDLIADI PEEIRLKKSL DLAPALDEMA VRRQLESLAA
     RNRSTAGYVS FLGGGAYDQF IPSAIRAIVS RSEFYTAYTP YQAEVSQGTL QAIYEYQSLI
     CRLYGMDVAN ASMYDGATAL AEAALMAMNV TGKERIVVAG QLHPWNSSVL STYLGAAGHS
     PVVQNSVEEG VGSIASLRGM VDGTVAAVIV QQPNFYGCLE DVEAIGAIAR EAGALFIVSA
     DPHSLGVLEA PGAYGADIAV GEGQPLGSAQ SFGGPYLGIF TVREKFVRKI PGRLVGMTKD
     RDGRDGFILT LQTREQHIRR EKATSNICTN QALNALQAAV YLSLLGRQGM QEVAGQSLER
     AHYLAARIVE IPGYSLRFSA PFFREFVLNT PVHPAVIVER MLEEGIFAGI DLSVFGDEGL
     LVSVTEKRTK EEMDRFALLL SSF
//